Magnesium in PDB 8beo: Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Enzymatic activity of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
All present enzymatic activity of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map:
4.1.1.47;
Protein crystallography data
The structure of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map, PDB code: 8beo
was solved by
B.Shaanan,
E.Binshtein,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.35 /
1.96
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
188.641,
188.641,
246.957,
90,
90,
90
|
R / Rfree (%)
|
17.6 /
20.4
|
Other elements in 8beo:
The structure of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map also contains other interesting chemical elements:
Magnesium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
13;
Binding sites:
The binding sites of Magnesium atom in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
(pdb code 8beo). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 13 binding sites of Magnesium where determined in the
Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map, PDB code: 8beo:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 1 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg601
b:18.1
occ:1.00
|
OD1
|
A:ASN473
|
2.0
|
20.7
|
1.0
|
O1A
|
A:TDK604
|
2.0
|
19.4
|
1.0
|
OD1
|
A:ASP446
|
2.1
|
20.1
|
1.0
|
O1B
|
A:TDK604
|
2.1
|
18.9
|
1.0
|
O
|
A:TYR475
|
2.1
|
18.3
|
1.0
|
O
|
A:HOH880
|
2.1
|
17.9
|
1.0
|
HD21
|
A:ASN473
|
2.9
|
20.6
|
1.0
|
CG
|
A:ASN473
|
3.0
|
21.9
|
1.0
|
H
|
A:TYR475
|
3.1
|
18.3
|
1.0
|
H
|
A:ASP446
|
3.1
|
20.2
|
1.0
|
H
|
A:GLY477
|
3.2
|
20.9
|
1.0
|
CG
|
A:ASP446
|
3.2
|
20.7
|
1.0
|
PA
|
A:TDK604
|
3.3
|
20.7
|
1.0
|
C
|
A:TYR475
|
3.3
|
19.1
|
1.0
|
PB
|
A:TDK604
|
3.3
|
20.1
|
1.0
|
ND2
|
A:ASN473
|
3.3
|
20.4
|
1.0
|
H
|
A:ASN473
|
3.4
|
19.6
|
1.0
|
O3A
|
A:TDK604
|
3.5
|
19.1
|
1.0
|
H
|
A:PHE447
|
3.7
|
19.6
|
1.0
|
OD2
|
A:ASP446
|
3.8
|
21.6
|
1.0
|
N
|
A:TYR475
|
3.9
|
18.4
|
1.0
|
N
|
A:ASP446
|
3.9
|
20.1
|
1.0
|
HA3
|
A:GLY445
|
3.9
|
19.5
|
1.0
|
O2B
|
A:TDK604
|
3.9
|
20.6
|
1.0
|
O7
|
A:TDK604
|
4.0
|
21.4
|
1.0
|
CA
|
A:TYR475
|
4.0
|
18.9
|
1.0
|
HA
|
A:LEU476
|
4.1
|
19.5
|
1.0
|
N
|
A:GLY477
|
4.1
|
21.0
|
1.0
|
HB2
|
A:TYR475
|
4.1
|
19.1
|
1.0
|
HD22
|
A:ASN473
|
4.2
|
21.2
|
1.0
|
N
|
A:ASN473
|
4.2
|
20.0
|
1.0
|
HB3
|
A:TYR475
|
4.2
|
18.9
|
1.0
|
CB
|
A:ASN473
|
4.3
|
20.5
|
1.0
|
N
|
A:LEU476
|
4.3
|
19.8
|
1.0
|
H11
|
A:PEG608
|
4.4
|
21.8
|
0.8
|
CB
|
A:ASP446
|
4.4
|
19.9
|
1.0
|
CB
|
A:TYR475
|
4.4
|
19.1
|
1.0
|
HB2
|
A:PHE447
|
4.4
|
19.4
|
1.0
|
H
|
A:ALA474
|
4.5
|
18.8
|
1.0
|
HA2
|
A:GLY445
|
4.5
|
19.7
|
1.0
|
HA3
|
A:GLY477
|
4.5
|
21.4
|
1.0
|
N
|
A:PHE447
|
4.5
|
19.4
|
1.0
|
CA
|
A:GLY445
|
4.5
|
19.5
|
1.0
|
HD11
|
A:LEU494
|
4.5
|
19.6
|
1.0
|
O
|
A:VAL471
|
4.6
|
19.5
|
1.0
|
O2A
|
A:TDK604
|
4.6
|
19.5
|
1.0
|
HA
|
A:ASN472
|
4.6
|
19.2
|
1.0
|
CA
|
A:LEU476
|
4.6
|
19.3
|
1.0
|
O3B
|
A:TDK604
|
4.6
|
18.9
|
1.0
|
CA
|
A:ASP446
|
4.6
|
19.9
|
1.0
|
N
|
A:ALA474
|
4.6
|
18.8
|
1.0
|
CA
|
A:ASN473
|
4.6
|
20.5
|
1.0
|
C
|
A:GLY445
|
4.7
|
19.7
|
1.0
|
HB3
|
A:ASP446
|
4.7
|
20.3
|
1.0
|
C
|
A:ASN473
|
4.8
|
20.3
|
1.0
|
H12
|
A:PEG608
|
4.8
|
21.8
|
0.8
|
HB3
|
A:ASN473
|
4.8
|
20.9
|
1.0
|
C
|
A:LEU476
|
4.9
|
20.9
|
1.0
|
CA
|
A:GLY477
|
4.9
|
21.6
|
1.0
|
HB2
|
A:ASN473
|
4.9
|
21.1
|
1.0
|
HA
|
A:TYR475
|
5.0
|
19.1
|
1.0
|
|
Magnesium binding site 2 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 2 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg602
b:22.0
occ:0.50
|
OE1
|
A:GLU454
|
2.4
|
18.7
|
1.0
|
O
|
A:PHE451
|
2.4
|
17.4
|
1.0
|
HA
|
A:LEU452
|
2.7
|
17.7
|
1.0
|
HD23
|
A:LEU452
|
2.9
|
17.4
|
1.0
|
CD
|
A:GLU454
|
3.3
|
18.8
|
1.0
|
C
|
A:PHE451
|
3.5
|
17.5
|
1.0
|
OE2
|
A:GLU454
|
3.6
|
18.1
|
1.0
|
CA
|
A:LEU452
|
3.7
|
17.8
|
1.0
|
HD1
|
A:HIS50
|
3.7
|
15.0
|
0.0
|
CD2
|
A:LEU452
|
3.8
|
17.3
|
1.0
|
H
|
A:ILE453
|
3.9
|
18.3
|
1.0
|
HD21
|
A:LEU452
|
4.0
|
17.4
|
1.0
|
N
|
A:LEU452
|
4.0
|
18.1
|
1.0
|
H
|
A:GLU454
|
4.1
|
18.6
|
1.0
|
HG21
|
A:ILE453
|
4.4
|
20.0
|
1.0
|
HD22
|
A:LEU452
|
4.4
|
17.3
|
1.0
|
C
|
A:LEU452
|
4.4
|
17.4
|
1.0
|
N
|
A:ILE453
|
4.4
|
18.8
|
1.0
|
O
|
A:GLN450
|
4.4
|
18.1
|
1.0
|
ND1
|
A:HIS50
|
4.5
|
17.8
|
1.0
|
CG
|
A:GLU454
|
4.5
|
18.0
|
1.0
|
HG3
|
A:GLU454
|
4.6
|
18.3
|
1.0
|
CB
|
A:LEU452
|
4.7
|
16.8
|
1.0
|
CG
|
A:LEU452
|
4.7
|
17.2
|
1.0
|
HA
|
A:PHE451
|
4.7
|
17.1
|
1.0
|
HB3
|
A:GLU454
|
4.7
|
18.3
|
1.0
|
CA
|
A:PHE451
|
4.8
|
16.6
|
1.0
|
HB2
|
A:HIS50
|
4.8
|
17.4
|
1.0
|
HG
|
A:LEU452
|
4.8
|
17.2
|
1.0
|
H
|
A:LEU452
|
4.9
|
17.9
|
1.0
|
HB3
|
A:LEU452
|
4.9
|
17.1
|
1.0
|
|
Magnesium binding site 3 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 3 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg624
b:32.0
occ:1.00
|
H
|
A:PHE407
|
2.1
|
26.3
|
1.0
|
O
|
A:ARG385
|
2.7
|
27.6
|
1.0
|
O
|
A:VAL387
|
2.9
|
23.0
|
1.0
|
N
|
A:PHE407
|
2.9
|
26.7
|
1.0
|
HA
|
A:VAL406
|
3.1
|
25.9
|
1.0
|
HD1
|
A:PHE407
|
3.1
|
23.5
|
1.0
|
HB3
|
A:HIS411
|
3.1
|
23.5
|
1.0
|
HD1
|
A:HIS411
|
3.2
|
24.5
|
0.0
|
HB2
|
A:PHE407
|
3.2
|
25.4
|
1.0
|
HB
|
A:VAL406
|
3.3
|
28.0
|
1.0
|
H
|
A:LYS408
|
3.3
|
28.1
|
1.0
|
HG3
|
A:LYS408
|
3.4
|
41.5
|
1.0
|
HB2
|
A:HIS411
|
3.4
|
23.6
|
1.0
|
HG11
|
A:VAL387
|
3.5
|
26.1
|
1.0
|
ND1
|
A:HIS411
|
3.6
|
27.4
|
1.0
|
CB
|
A:HIS411
|
3.6
|
23.5
|
1.0
|
C
|
A:ARG385
|
3.7
|
26.4
|
1.0
|
CA
|
A:VAL406
|
3.7
|
26.3
|
1.0
|
N
|
A:LYS408
|
3.8
|
28.5
|
1.0
|
CA
|
A:PHE407
|
3.8
|
26.9
|
1.0
|
C
|
A:VAL406
|
3.8
|
25.9
|
1.0
|
HA
|
A:ASP386
|
3.8
|
28.0
|
1.0
|
CB
|
A:PHE407
|
3.9
|
25.4
|
1.0
|
CD1
|
A:PHE407
|
3.9
|
24.1
|
1.0
|
CG
|
A:HIS411
|
3.9
|
24.5
|
1.0
|
CB
|
A:VAL406
|
4.0
|
27.5
|
1.0
|
C
|
A:VAL387
|
4.0
|
22.3
|
1.0
|
H
|
A:VAL387
|
4.0
|
25.7
|
1.0
|
N
|
A:VAL387
|
4.0
|
25.2
|
1.0
|
HB2
|
A:LYS408
|
4.1
|
34.9
|
1.0
|
C
|
A:PHE407
|
4.1
|
27.5
|
1.0
|
C
|
A:ASP386
|
4.2
|
26.8
|
1.0
|
HG13
|
A:VAL387
|
4.2
|
25.5
|
1.0
|
CG1
|
A:VAL387
|
4.3
|
25.9
|
1.0
|
CG
|
A:LYS408
|
4.3
|
42.0
|
1.0
|
CA
|
A:ASP386
|
4.3
|
28.4
|
1.0
|
CG
|
A:PHE407
|
4.4
|
24.4
|
1.0
|
HA
|
A:ARG385
|
4.4
|
28.4
|
1.0
|
N
|
A:ASP386
|
4.4
|
26.4
|
1.0
|
CB
|
A:LYS408
|
4.5
|
35.4
|
1.0
|
CA
|
A:VAL387
|
4.6
|
24.2
|
1.0
|
HG11
|
A:VAL406
|
4.6
|
30.1
|
1.0
|
O
|
A:ASP386
|
4.7
|
26.5
|
1.0
|
CE1
|
A:HIS411
|
4.7
|
27.4
|
1.0
|
HA
|
A:PHE407
|
4.7
|
26.8
|
1.0
|
CA
|
A:ARG385
|
4.7
|
28.9
|
1.0
|
CA
|
A:LYS408
|
4.7
|
29.9
|
1.0
|
HB3
|
A:PHE407
|
4.7
|
25.9
|
1.0
|
HE2
|
A:LYS408
|
4.8
|
52.4
|
1.0
|
HG23
|
A:VAL406
|
4.8
|
27.9
|
1.0
|
O
|
A:LYS408
|
4.8
|
21.9
|
1.0
|
HA
|
A:CYS388
|
4.8
|
20.2
|
1.0
|
HG2
|
A:LYS408
|
4.9
|
41.9
|
1.0
|
CG1
|
A:VAL406
|
4.9
|
31.5
|
1.0
|
O
|
A:HIS405
|
4.9
|
21.6
|
1.0
|
HD2
|
A:LYS408
|
4.9
|
46.6
|
1.0
|
HG12
|
A:VAL387
|
5.0
|
26.0
|
1.0
|
|
Magnesium binding site 4 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 4 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg601
b:21.2
occ:1.00
|
O1A
|
B:TDK604
|
1.9
|
22.8
|
1.0
|
OD1
|
B:ASP446
|
2.1
|
23.1
|
1.0
|
O1B
|
B:TDK604
|
2.1
|
21.3
|
1.0
|
O
|
B:TYR475
|
2.1
|
21.5
|
1.0
|
OD1
|
B:ASN473
|
2.1
|
21.8
|
1.0
|
O
|
B:HOH837
|
2.1
|
21.4
|
1.0
|
H
|
B:ASP446
|
3.0
|
21.4
|
1.0
|
HD21
|
B:ASN473
|
3.0
|
22.1
|
1.0
|
CG
|
B:ASN473
|
3.1
|
22.5
|
1.0
|
H
|
B:TYR475
|
3.1
|
22.8
|
1.0
|
CG
|
B:ASP446
|
3.2
|
22.2
|
1.0
|
PA
|
B:TDK604
|
3.2
|
23.6
|
1.0
|
PB
|
B:TDK604
|
3.3
|
22.7
|
1.0
|
H
|
B:GLY477
|
3.3
|
24.5
|
1.0
|
C
|
B:TYR475
|
3.3
|
22.3
|
1.0
|
H
|
B:ASN473
|
3.4
|
22.1
|
1.0
|
O3A
|
B:TDK604
|
3.4
|
23.8
|
1.0
|
ND2
|
B:ASN473
|
3.4
|
22.4
|
1.0
|
H
|
B:PHE447
|
3.5
|
20.8
|
1.0
|
OD2
|
B:ASP446
|
3.7
|
22.4
|
1.0
|
HA3
|
B:GLY445
|
3.8
|
21.0
|
1.0
|
N
|
B:ASP446
|
3.8
|
20.7
|
1.0
|
N
|
B:TYR475
|
3.9
|
23.1
|
1.0
|
O2B
|
B:TDK604
|
3.9
|
22.1
|
1.0
|
O7
|
B:TDK604
|
3.9
|
25.3
|
1.0
|
HA
|
B:LEU476
|
4.1
|
22.7
|
1.0
|
CA
|
B:TYR475
|
4.1
|
23.3
|
1.0
|
N
|
B:GLY477
|
4.1
|
24.9
|
1.0
|
HB2
|
B:TYR475
|
4.2
|
23.2
|
1.0
|
HB3
|
B:TYR475
|
4.2
|
22.9
|
1.0
|
N
|
B:ASN473
|
4.2
|
22.7
|
1.0
|
HB2
|
B:PHE447
|
4.3
|
19.9
|
1.0
|
HD22
|
B:ASN473
|
4.3
|
22.6
|
1.0
|
CB
|
B:ASP446
|
4.4
|
21.3
|
1.0
|
N
|
B:LEU476
|
4.4
|
22.6
|
1.0
|
N
|
B:PHE447
|
4.4
|
21.0
|
1.0
|
CA
|
B:GLY445
|
4.4
|
21.0
|
1.0
|
HA2
|
B:GLY445
|
4.4
|
21.2
|
1.0
|
O2A
|
B:TDK604
|
4.4
|
20.1
|
1.0
|
CB
|
B:TYR475
|
4.4
|
22.9
|
1.0
|
CB
|
B:ASN473
|
4.5
|
22.1
|
1.0
|
H
|
B:ALA474
|
4.5
|
23.9
|
1.0
|
O
|
B:VAL471
|
4.5
|
20.1
|
1.0
|
HD11
|
B:LEU494
|
4.5
|
21.3
|
1.0
|
O3B
|
B:TDK604
|
4.5
|
21.0
|
1.0
|
C
|
B:GLY445
|
4.5
|
21.7
|
1.0
|
CA
|
B:ASP446
|
4.6
|
21.3
|
1.0
|
HA
|
B:ASN472
|
4.6
|
20.7
|
1.0
|
HA3
|
B:GLY477
|
4.6
|
25.4
|
1.0
|
CA
|
B:LEU476
|
4.6
|
22.8
|
1.0
|
N
|
B:ALA474
|
4.7
|
24.5
|
1.0
|
CA
|
B:ASN473
|
4.7
|
23.3
|
1.0
|
HB3
|
B:ASP446
|
4.7
|
21.8
|
1.0
|
C
|
B:ASN473
|
4.8
|
24.5
|
1.0
|
C
|
B:LEU476
|
4.9
|
24.2
|
1.0
|
CA
|
B:GLY477
|
4.9
|
25.4
|
1.0
|
HB2
|
B:ASN473
|
5.0
|
22.9
|
1.0
|
|
Magnesium binding site 5 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 5 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg602
b:20.8
occ:0.50
|
O
|
B:PHE451
|
2.4
|
19.8
|
1.0
|
OE1
|
B:GLU454
|
2.4
|
17.9
|
1.0
|
HA
|
B:LEU452
|
2.8
|
18.4
|
1.0
|
HD23
|
B:LEU452
|
3.0
|
20.9
|
1.0
|
CD
|
B:GLU454
|
3.3
|
19.0
|
1.0
|
C
|
B:PHE451
|
3.5
|
18.5
|
1.0
|
CA
|
B:LEU452
|
3.7
|
18.0
|
1.0
|
OE2
|
B:GLU454
|
3.7
|
19.1
|
1.0
|
HD1
|
B:HIS50
|
3.8
|
17.9
|
0.0
|
CD2
|
B:LEU452
|
3.9
|
21.4
|
1.0
|
H
|
B:ILE453
|
3.9
|
19.5
|
1.0
|
HD21
|
B:LEU452
|
3.9
|
20.9
|
1.0
|
N
|
B:LEU452
|
4.0
|
17.8
|
1.0
|
H
|
B:GLU454
|
4.0
|
20.0
|
1.0
|
O
|
B:GLN450
|
4.3
|
19.8
|
1.0
|
HG21
|
B:ILE453
|
4.3
|
19.6
|
1.0
|
C
|
B:LEU452
|
4.4
|
18.6
|
1.0
|
N
|
B:ILE453
|
4.4
|
20.1
|
1.0
|
HD22
|
B:LEU452
|
4.4
|
20.7
|
1.0
|
CG
|
B:GLU454
|
4.5
|
18.9
|
1.0
|
ND1
|
B:HIS50
|
4.6
|
21.2
|
1.0
|
HG3
|
B:GLU454
|
4.6
|
19.3
|
1.0
|
HB3
|
B:GLU454
|
4.6
|
20.0
|
1.0
|
HA
|
B:PHE451
|
4.6
|
18.6
|
1.0
|
CB
|
B:LEU452
|
4.7
|
18.9
|
1.0
|
CA
|
B:PHE451
|
4.7
|
18.1
|
1.0
|
CG
|
B:LEU452
|
4.7
|
19.4
|
1.0
|
HB2
|
B:HIS50
|
4.8
|
19.1
|
1.0
|
HG
|
B:LEU452
|
4.9
|
19.8
|
1.0
|
H
|
B:LEU452
|
4.9
|
17.9
|
1.0
|
N
|
B:GLU454
|
4.9
|
20.4
|
1.0
|
HB3
|
B:LEU452
|
5.0
|
18.8
|
1.0
|
|
Magnesium binding site 6 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 6 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg622
b:46.2
occ:1.00
|
HB3
|
B:ASN283
|
2.7
|
25.2
|
1.0
|
HG12
|
B:VAL311
|
3.6
|
30.9
|
1.0
|
CB
|
B:ASN283
|
3.6
|
25.2
|
1.0
|
H
|
B:ASN283
|
3.9
|
24.2
|
1.0
|
HB2
|
B:ASN283
|
4.1
|
25.4
|
1.0
|
CG
|
B:ASN283
|
4.1
|
25.2
|
1.0
|
HG11
|
B:VAL311
|
4.1
|
31.4
|
1.0
|
OD1
|
B:ASN283
|
4.2
|
25.8
|
1.0
|
CG1
|
B:VAL311
|
4.3
|
31.7
|
1.0
|
O
|
B:HOH843
|
4.4
|
29.7
|
1.0
|
N
|
B:ASN283
|
4.4
|
23.8
|
1.0
|
CA
|
B:ASN283
|
4.5
|
24.2
|
1.0
|
HB
|
B:VAL311
|
4.6
|
30.7
|
1.0
|
HA
|
B:ASN283
|
4.6
|
24.4
|
1.0
|
|
Magnesium binding site 7 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 7 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg601
b:25.7
occ:1.00
|
O
|
C:TYR475
|
2.0
|
25.1
|
1.0
|
OD1
|
C:ASN473
|
2.0
|
28.8
|
1.0
|
O1A
|
C:TDK603
|
2.0
|
24.9
|
1.0
|
O1B
|
C:TDK603
|
2.1
|
26.6
|
1.0
|
OD1
|
C:ASP446
|
2.1
|
30.0
|
1.0
|
O
|
C:HOH862
|
2.2
|
25.4
|
1.0
|
CG
|
C:ASN473
|
3.0
|
29.8
|
1.0
|
H
|
C:ASP446
|
3.1
|
27.3
|
1.0
|
H
|
C:TYR475
|
3.1
|
26.3
|
1.0
|
HD21
|
C:ASN473
|
3.2
|
30.0
|
1.0
|
H
|
C:GLY477
|
3.2
|
28.2
|
1.0
|
PA
|
C:TDK603
|
3.2
|
27.7
|
1.0
|
C
|
C:TYR475
|
3.2
|
27.0
|
1.0
|
CG
|
C:ASP446
|
3.3
|
29.3
|
1.0
|
PB
|
C:TDK603
|
3.3
|
28.8
|
1.0
|
ND2
|
C:ASN473
|
3.4
|
30.4
|
1.0
|
H
|
C:ASN473
|
3.4
|
27.7
|
1.0
|
O3A
|
C:TDK603
|
3.5
|
27.4
|
1.0
|
H
|
C:PHE447
|
3.6
|
25.7
|
1.0
|
OD2
|
C:ASP446
|
3.8
|
28.6
|
1.0
|
N
|
C:TYR475
|
3.8
|
26.6
|
1.0
|
N
|
C:ASP446
|
3.9
|
26.8
|
1.0
|
O7
|
C:TDK603
|
3.9
|
29.9
|
1.0
|
HA3
|
C:GLY445
|
3.9
|
28.1
|
1.0
|
O2B
|
C:TDK603
|
3.9
|
27.4
|
1.0
|
CA
|
C:TYR475
|
4.0
|
27.4
|
1.0
|
N
|
C:GLY477
|
4.0
|
28.3
|
1.0
|
HA
|
C:LEU476
|
4.0
|
26.3
|
1.0
|
HD22
|
C:ASN473
|
4.1
|
30.4
|
1.0
|
HB2
|
C:TYR475
|
4.1
|
28.2
|
1.0
|
HB3
|
C:TYR475
|
4.1
|
28.0
|
1.0
|
N
|
C:ASN473
|
4.3
|
27.5
|
1.0
|
N
|
C:LEU476
|
4.3
|
26.8
|
1.0
|
CB
|
C:TYR475
|
4.3
|
28.3
|
1.0
|
HB2
|
C:PHE447
|
4.4
|
26.2
|
1.0
|
CB
|
C:ASN473
|
4.4
|
28.8
|
1.0
|
CB
|
C:ASP446
|
4.4
|
27.8
|
1.0
|
H
|
C:ALA474
|
4.4
|
26.7
|
1.0
|
HA3
|
C:GLY477
|
4.5
|
30.0
|
1.0
|
N
|
C:PHE447
|
4.5
|
25.4
|
1.0
|
O2A
|
C:TDK603
|
4.5
|
26.0
|
1.0
|
HD11
|
C:LEU494
|
4.5
|
25.9
|
1.0
|
O3B
|
C:TDK603
|
4.5
|
25.6
|
1.0
|
CA
|
C:LEU476
|
4.6
|
26.3
|
1.0
|
CA
|
C:GLY445
|
4.6
|
28.3
|
1.0
|
HA2
|
C:GLY445
|
4.6
|
28.4
|
1.0
|
HA
|
C:ASN472
|
4.6
|
28.0
|
1.0
|
CA
|
C:ASP446
|
4.6
|
27.5
|
1.0
|
N
|
C:ALA474
|
4.6
|
26.6
|
1.0
|
O
|
C:VAL471
|
4.6
|
25.9
|
1.0
|
C
|
C:GLY445
|
4.7
|
27.7
|
1.0
|
CA
|
C:ASN473
|
4.7
|
28.8
|
1.0
|
C
|
C:ASN473
|
4.8
|
28.4
|
1.0
|
HB3
|
C:ASP446
|
4.8
|
28.3
|
1.0
|
CA
|
C:GLY477
|
4.8
|
30.4
|
1.0
|
C
|
C:LEU476
|
4.8
|
26.9
|
1.0
|
HB3
|
C:ASN473
|
4.9
|
29.2
|
1.0
|
HA
|
C:TYR475
|
4.9
|
27.5
|
1.0
|
HB2
|
C:ASN473
|
4.9
|
29.4
|
1.0
|
|
Magnesium binding site 8 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 8 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg605
b:22.6
occ:1.00
|
OE1
|
E:GLU454
|
2.3
|
26.1
|
1.0
|
O
|
C:PHE451
|
2.3
|
27.0
|
1.0
|
OE1
|
C:GLU454
|
2.4
|
27.9
|
1.0
|
O
|
E:PHE451
|
2.4
|
26.1
|
1.0
|
HA
|
C:LEU452
|
2.7
|
26.5
|
1.0
|
HA
|
E:LEU452
|
2.8
|
25.5
|
1.0
|
HD23
|
E:LEU452
|
2.9
|
27.2
|
1.0
|
HD23
|
C:LEU452
|
2.9
|
26.4
|
1.0
|
CD
|
E:GLU454
|
3.2
|
27.9
|
1.0
|
CD
|
C:GLU454
|
3.3
|
29.3
|
1.0
|
C
|
C:PHE451
|
3.4
|
26.6
|
1.0
|
C
|
E:PHE451
|
3.5
|
26.5
|
1.0
|
CA
|
C:LEU452
|
3.6
|
25.9
|
1.0
|
OE2
|
C:GLU454
|
3.6
|
28.6
|
1.0
|
OE2
|
E:GLU454
|
3.7
|
26.9
|
1.0
|
CA
|
E:LEU452
|
3.7
|
25.3
|
1.0
|
HD1
|
E:HIS50
|
3.7
|
24.4
|
0.0
|
HD2
|
C:HIS50
|
3.8
|
24.4
|
1.0
|
CD2
|
E:LEU452
|
3.8
|
27.5
|
1.0
|
HD21
|
E:LEU452
|
3.8
|
27.1
|
1.0
|
CD2
|
C:LEU452
|
3.8
|
26.5
|
1.0
|
HD21
|
C:LEU452
|
3.9
|
26.3
|
1.0
|
H
|
E:ILE453
|
3.9
|
26.3
|
1.0
|
H
|
C:ILE453
|
3.9
|
27.1
|
1.0
|
N
|
C:LEU452
|
4.0
|
26.9
|
1.0
|
H
|
E:GLU454
|
4.0
|
27.2
|
1.0
|
N
|
E:LEU452
|
4.1
|
25.4
|
1.0
|
H
|
C:GLU454
|
4.1
|
27.6
|
1.0
|
HG21
|
C:ILE453
|
4.3
|
29.0
|
1.0
|
HG21
|
E:ILE453
|
4.3
|
27.4
|
1.0
|
HD22
|
E:LEU452
|
4.3
|
27.0
|
1.0
|
C
|
C:LEU452
|
4.4
|
26.4
|
1.0
|
C
|
E:LEU452
|
4.4
|
25.5
|
1.0
|
O
|
C:GLN450
|
4.4
|
26.2
|
1.0
|
N
|
E:ILE453
|
4.4
|
26.5
|
1.0
|
N
|
C:ILE453
|
4.4
|
27.0
|
1.0
|
HD22
|
C:LEU452
|
4.4
|
26.2
|
1.0
|
CG
|
E:GLU454
|
4.4
|
27.7
|
1.0
|
O
|
E:GLN450
|
4.5
|
25.1
|
1.0
|
ND1
|
E:HIS50
|
4.5
|
29.6
|
1.0
|
CG
|
C:GLU454
|
4.5
|
28.6
|
1.0
|
HB3
|
E:GLU454
|
4.5
|
27.6
|
1.0
|
HG3
|
E:GLU454
|
4.5
|
27.7
|
1.0
|
HG3
|
C:GLU454
|
4.5
|
28.9
|
1.0
|
CD2
|
C:HIS50
|
4.6
|
24.4
|
1.0
|
HA
|
C:PHE451
|
4.6
|
26.9
|
1.0
|
CB
|
C:LEU452
|
4.7
|
26.7
|
1.0
|
HB3
|
C:GLU454
|
4.7
|
28.3
|
1.0
|
CB
|
E:LEU452
|
4.7
|
25.7
|
1.0
|
HA
|
E:PHE451
|
4.7
|
26.4
|
1.0
|
CG
|
C:LEU452
|
4.7
|
25.6
|
1.0
|
CA
|
C:PHE451
|
4.7
|
26.9
|
1.0
|
CG
|
E:LEU452
|
4.7
|
26.2
|
1.0
|
CA
|
E:PHE451
|
4.8
|
25.8
|
1.0
|
HB2
|
E:HIS50
|
4.8
|
26.1
|
1.0
|
HG
|
C:LEU452
|
4.8
|
25.9
|
1.0
|
HG
|
E:LEU452
|
4.8
|
26.4
|
1.0
|
HB2
|
C:HIS50
|
4.9
|
26.1
|
1.0
|
H
|
C:LEU452
|
4.9
|
26.5
|
1.0
|
N
|
E:GLU454
|
4.9
|
27.4
|
1.0
|
HB3
|
C:LEU452
|
4.9
|
26.3
|
1.0
|
HB3
|
E:LEU452
|
4.9
|
25.7
|
1.0
|
H
|
E:LEU452
|
5.0
|
25.6
|
1.0
|
N
|
C:GLU454
|
5.0
|
27.9
|
1.0
|
|
Magnesium binding site 9 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 9 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg601
b:28.0
occ:1.00
|
O1B
|
D:TDK603
|
2.0
|
27.2
|
1.0
|
O
|
D:TYR475
|
2.1
|
27.0
|
1.0
|
O1A
|
D:TDK603
|
2.1
|
28.5
|
1.0
|
OD1
|
D:ASP446
|
2.1
|
28.1
|
1.0
|
OD1
|
D:ASN473
|
2.2
|
30.6
|
1.0
|
O
|
D:HOH834
|
2.2
|
26.2
|
1.0
|
CG
|
D:ASN473
|
3.0
|
31.6
|
1.0
|
HD21
|
D:ASN473
|
3.1
|
31.4
|
1.0
|
H
|
D:ASP446
|
3.1
|
29.1
|
1.0
|
H
|
D:TYR475
|
3.2
|
28.4
|
1.0
|
H
|
D:GLY477
|
3.2
|
27.6
|
1.0
|
PB
|
D:TDK603
|
3.2
|
27.6
|
1.0
|
CG
|
D:ASP446
|
3.3
|
30.2
|
1.0
|
PA
|
D:TDK603
|
3.3
|
29.2
|
1.0
|
C
|
D:TYR475
|
3.3
|
28.8
|
1.0
|
ND2
|
D:ASN473
|
3.3
|
31.8
|
1.0
|
H
|
D:ASN473
|
3.4
|
30.3
|
1.0
|
O3A
|
D:TDK603
|
3.5
|
28.7
|
1.0
|
H
|
D:PHE447
|
3.6
|
29.6
|
1.0
|
OD2
|
D:ASP446
|
3.8
|
30.1
|
1.0
|
HA3
|
D:GLY445
|
3.8
|
30.0
|
1.0
|
N
|
D:ASP446
|
3.9
|
28.1
|
1.0
|
N
|
D:TYR475
|
3.9
|
28.4
|
1.0
|
O2B
|
D:TDK603
|
3.9
|
29.1
|
1.0
|
O7
|
D:TDK603
|
4.0
|
31.4
|
1.0
|
N
|
D:GLY477
|
4.1
|
27.4
|
1.0
|
HA
|
D:LEU476
|
4.1
|
28.5
|
1.0
|
CA
|
D:TYR475
|
4.1
|
30.0
|
1.0
|
HD22
|
D:ASN473
|
4.1
|
31.9
|
1.0
|
HB2
|
D:TYR475
|
4.2
|
30.9
|
1.0
|
HB3
|
D:TYR475
|
4.2
|
30.6
|
1.0
|
N
|
D:ASN473
|
4.3
|
30.9
|
1.0
|
N
|
D:LEU476
|
4.3
|
28.9
|
1.0
|
CB
|
D:ASN473
|
4.4
|
30.8
|
1.0
|
O3B
|
D:TDK603
|
4.4
|
27.4
|
1.0
|
HB2
|
D:PHE447
|
4.4
|
29.6
|
1.0
|
CB
|
D:TYR475
|
4.4
|
30.7
|
1.0
|
CB
|
D:ASP446
|
4.4
|
30.2
|
1.0
|
HA2
|
D:GLY445
|
4.5
|
30.2
|
1.0
|
CA
|
D:GLY445
|
4.5
|
30.1
|
1.0
|
HA3
|
D:GLY477
|
4.5
|
28.5
|
1.0
|
N
|
D:PHE447
|
4.5
|
29.3
|
1.0
|
H
|
D:ALA474
|
4.5
|
29.5
|
1.0
|
HA
|
D:ASN472
|
4.6
|
29.6
|
1.0
|
O2A
|
D:TDK603
|
4.6
|
28.1
|
1.0
|
HD11
|
D:LEU494
|
4.6
|
31.0
|
1.0
|
O
|
D:VAL471
|
4.6
|
29.5
|
1.0
|
C
|
D:GLY445
|
4.6
|
29.8
|
1.0
|
CA
|
D:LEU476
|
4.6
|
28.8
|
1.0
|
CA
|
D:ASP446
|
4.6
|
29.2
|
1.0
|
N
|
D:ALA474
|
4.7
|
29.6
|
1.0
|
CA
|
D:ASN473
|
4.7
|
30.4
|
1.0
|
HB3
|
D:ASP446
|
4.8
|
30.2
|
1.0
|
C
|
D:ASN473
|
4.8
|
30.8
|
1.0
|
CA
|
D:GLY477
|
4.9
|
28.5
|
1.0
|
C
|
D:LEU476
|
4.9
|
28.6
|
1.0
|
HB3
|
D:ASN473
|
4.9
|
31.0
|
1.0
|
HB2
|
D:ASN473
|
5.0
|
31.4
|
1.0
|
HA
|
D:TYR475
|
5.0
|
29.9
|
1.0
|
|
Magnesium binding site 10 out
of 13 in 8beo
Go back to
Magnesium Binding Sites List in 8beo
Magnesium binding site 10 out
of 13 in the Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 10 of Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg601
b:29.5
occ:1.00
|
O
|
E:TYR475
|
2.0
|
26.0
|
1.0
|
O1B
|
E:TDK603
|
2.1
|
31.0
|
1.0
|
O1A
|
E:TDK603
|
2.1
|
32.9
|
1.0
|
OD1
|
E:ASP446
|
2.1
|
31.2
|
1.0
|
OD1
|
E:ASN473
|
2.1
|
28.7
|
1.0
|
O
|
E:HOH733
|
2.3
|
24.7
|
1.0
|
CG
|
E:ASN473
|
3.1
|
30.9
|
1.0
|
H
|
E:TYR475
|
3.1
|
29.9
|
1.0
|
HD21
|
E:ASN473
|
3.1
|
31.6
|
1.0
|
H
|
E:ASP446
|
3.1
|
30.9
|
1.0
|
PA
|
E:TDK603
|
3.2
|
32.3
|
1.0
|
CG
|
E:ASP446
|
3.2
|
30.8
|
1.0
|
C
|
E:TYR475
|
3.2
|
28.6
|
1.0
|
PB
|
E:TDK603
|
3.2
|
33.0
|
1.0
|
H
|
E:GLY477
|
3.3
|
32.0
|
1.0
|
ND2
|
E:ASN473
|
3.4
|
32.2
|
1.0
|
O3A
|
E:TDK603
|
3.4
|
34.0
|
1.0
|
H
|
E:ASN473
|
3.5
|
29.5
|
1.0
|
H
|
E:PHE447
|
3.6
|
28.1
|
1.0
|
OD2
|
E:ASP446
|
3.8
|
30.2
|
1.0
|
N
|
E:TYR475
|
3.8
|
30.3
|
1.0
|
N
|
E:ASP446
|
3.8
|
31.1
|
1.0
|
HA3
|
E:GLY445
|
3.9
|
30.3
|
1.0
|
O7
|
E:TDK603
|
3.9
|
36.7
|
1.0
|
O2B
|
E:TDK603
|
3.9
|
30.4
|
1.0
|
CA
|
E:TYR475
|
4.0
|
29.5
|
1.0
|
HA
|
E:LEU476
|
4.1
|
29.5
|
1.0
|
N
|
E:GLY477
|
4.1
|
32.4
|
1.0
|
HB2
|
E:TYR475
|
4.1
|
29.4
|
1.0
|
HD22
|
E:ASN473
|
4.2
|
32.1
|
1.0
|
HB3
|
E:TYR475
|
4.2
|
29.2
|
1.0
|
HB2
|
E:PHE447
|
4.3
|
26.8
|
1.0
|
N
|
E:LEU476
|
4.3
|
28.8
|
1.0
|
N
|
E:ASN473
|
4.3
|
29.6
|
1.0
|
CB
|
E:TYR475
|
4.4
|
29.1
|
1.0
|
CB
|
E:ASP446
|
4.4
|
30.1
|
1.0
|
N
|
E:PHE447
|
4.4
|
27.8
|
1.0
|
CB
|
E:ASN473
|
4.5
|
30.7
|
1.0
|
O2A
|
E:TDK603
|
4.5
|
31.7
|
1.0
|
HA2
|
E:GLY445
|
4.5
|
30.5
|
1.0
|
CA
|
E:GLY445
|
4.5
|
30.8
|
1.0
|
HD11
|
E:LEU494
|
4.5
|
32.2
|
1.0
|
HA3
|
E:GLY477
|
4.5
|
33.4
|
1.0
|
O3B
|
E:TDK603
|
4.5
|
30.7
|
1.0
|
H
|
E:ALA474
|
4.5
|
29.2
|
1.0
|
O
|
E:VAL471
|
4.6
|
28.4
|
1.0
|
C
|
E:GLY445
|
4.6
|
30.5
|
1.0
|
CA
|
E:ASP446
|
4.6
|
29.7
|
1.0
|
CA
|
E:LEU476
|
4.6
|
29.9
|
1.0
|
HA
|
E:ASN472
|
4.6
|
29.4
|
1.0
|
N
|
E:ALA474
|
4.7
|
28.9
|
1.0
|
CA
|
E:ASN473
|
4.8
|
30.2
|
1.0
|
HB3
|
E:ASP446
|
4.8
|
30.4
|
1.0
|
C
|
E:ASN473
|
4.8
|
29.8
|
1.0
|
C
|
E:LEU476
|
4.9
|
31.3
|
1.0
|
CA
|
E:GLY477
|
4.9
|
33.5
|
1.0
|
HA
|
E:TYR475
|
4.9
|
29.6
|
1.0
|
HB3
|
E:ASN473
|
5.0
|
30.8
|
1.0
|
|
Reference:
B.Shaanan,
E.Binshtein.
Crystal Structure of E. Coli Glyoxylate Carboligase Mutant I393A with Map To Be Published.
Page generated: Thu Oct 3 19:22:27 2024
|