Magnesium in PDB 1ozh: The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate.
Enzymatic activity of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate.
All present enzymatic activity of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate.:
4.1.3.18;
Protein crystallography data
The structure of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate., PDB code: 1ozh
was solved by
S.S.Pang,
R.G.Duggleby,
R.L.Schowen,
L.W.Guddat,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
100.00 /
2.00
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
86.320,
92.814,
97.420,
67.97,
63.48,
67.68
|
R / Rfree (%)
|
19.1 /
22.8
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate.
(pdb code 1ozh). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate., PDB code: 1ozh:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1ozh
Go back to
Magnesium Binding Sites List in 1ozh
Magnesium binding site 1 out
of 4 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1405
b:22.9
occ:1.00
|
OD1
|
A:ASP474
|
1.9
|
26.7
|
1.0
|
O
|
A:GLY476
|
2.0
|
25.0
|
1.0
|
O3B
|
A:HE31406
|
2.1
|
20.7
|
1.0
|
O2A
|
A:HE31406
|
2.1
|
19.9
|
1.0
|
O
|
A:HOH1435
|
2.2
|
25.6
|
1.0
|
OD1
|
A:ASP447
|
2.2
|
23.8
|
1.0
|
CG
|
A:ASP474
|
2.8
|
26.6
|
1.0
|
PB
|
A:HE31406
|
3.2
|
21.6
|
1.0
|
OD2
|
A:ASP474
|
3.2
|
26.4
|
1.0
|
PA
|
A:HE31406
|
3.2
|
23.0
|
1.0
|
C
|
A:GLY476
|
3.2
|
21.7
|
1.0
|
CG
|
A:ASP447
|
3.3
|
22.1
|
1.0
|
O1A
|
A:HE31406
|
3.4
|
22.9
|
1.0
|
O1B
|
A:HE31406
|
3.6
|
22.3
|
1.0
|
N
|
A:GLY476
|
3.7
|
23.8
|
1.0
|
O7
|
A:HE31406
|
3.8
|
20.3
|
1.0
|
OD2
|
A:ASP447
|
3.8
|
22.8
|
1.0
|
N
|
A:ASP447
|
3.9
|
18.3
|
1.0
|
CA
|
A:GLY476
|
4.0
|
23.1
|
1.0
|
CB
|
A:ASP474
|
4.1
|
26.1
|
1.0
|
N
|
A:ASN478
|
4.2
|
24.0
|
1.0
|
N
|
A:TYR477
|
4.2
|
21.8
|
1.0
|
N
|
A:GLY448
|
4.3
|
19.6
|
1.0
|
CA
|
A:TYR477
|
4.4
|
22.2
|
1.0
|
O2B
|
A:HE31406
|
4.4
|
21.3
|
1.0
|
N
|
A:ASP474
|
4.5
|
25.8
|
1.0
|
CZ
|
A:PHE496
|
4.5
|
26.2
|
1.0
|
O3A
|
A:HE31406
|
4.5
|
21.3
|
1.0
|
N
|
A:ASN475
|
4.5
|
26.4
|
1.0
|
CB
|
A:ASP447
|
4.6
|
20.2
|
1.0
|
O
|
A:TRP472
|
4.6
|
25.9
|
1.0
|
CA
|
A:GLY446
|
4.7
|
20.0
|
1.0
|
CA
|
A:ASP447
|
4.7
|
18.3
|
1.0
|
C
|
A:GLY446
|
4.7
|
21.1
|
1.0
|
CA
|
A:ASP474
|
4.8
|
26.4
|
1.0
|
CB
|
A:ASN478
|
4.8
|
25.7
|
1.0
|
C
|
A:ASP474
|
4.8
|
26.4
|
1.0
|
C
|
A:TYR477
|
4.8
|
22.4
|
1.0
|
C
|
A:ASN475
|
4.9
|
25.7
|
1.0
|
CE1
|
A:TYR543
|
5.0
|
24.8
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1ozh
Go back to
Magnesium Binding Sites List in 1ozh
Magnesium binding site 2 out
of 4 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1412
b:21.9
occ:1.00
|
OD1
|
B:ASP474
|
2.0
|
24.4
|
1.0
|
O
|
B:GLY476
|
2.0
|
17.6
|
1.0
|
O2A
|
B:HE31413
|
2.1
|
19.3
|
1.0
|
O3B
|
B:HE31413
|
2.1
|
18.1
|
1.0
|
OD1
|
B:ASP447
|
2.2
|
18.6
|
1.0
|
O
|
B:HOH1453
|
2.2
|
19.9
|
1.0
|
CG
|
B:ASP474
|
3.0
|
25.2
|
1.0
|
PA
|
B:HE31413
|
3.2
|
20.6
|
1.0
|
PB
|
B:HE31413
|
3.2
|
18.8
|
1.0
|
C
|
B:GLY476
|
3.2
|
20.6
|
1.0
|
CG
|
B:ASP447
|
3.3
|
21.3
|
1.0
|
O1A
|
B:HE31413
|
3.4
|
18.4
|
1.0
|
OD2
|
B:ASP474
|
3.4
|
22.1
|
1.0
|
O1B
|
B:HE31413
|
3.7
|
15.9
|
1.0
|
O7
|
B:HE31413
|
3.7
|
19.9
|
1.0
|
N
|
B:ASP447
|
3.8
|
18.0
|
1.0
|
OD2
|
B:ASP447
|
3.8
|
22.0
|
1.0
|
N
|
B:GLY476
|
3.8
|
20.6
|
1.0
|
CA
|
B:GLY476
|
4.1
|
20.2
|
1.0
|
N
|
B:GLY448
|
4.2
|
18.9
|
1.0
|
N
|
B:ASN478
|
4.2
|
21.8
|
1.0
|
N
|
B:TYR477
|
4.2
|
19.6
|
1.0
|
CB
|
B:ASP474
|
4.3
|
22.0
|
1.0
|
CA
|
B:TYR477
|
4.4
|
19.6
|
1.0
|
O3A
|
B:HE31413
|
4.5
|
19.4
|
1.0
|
CB
|
B:ASP447
|
4.5
|
18.9
|
1.0
|
O2B
|
B:HE31413
|
4.5
|
16.4
|
1.0
|
O
|
B:TRP472
|
4.5
|
19.0
|
1.0
|
CA
|
B:GLY446
|
4.5
|
18.8
|
1.0
|
N
|
B:ASP474
|
4.5
|
21.6
|
1.0
|
CA
|
B:ASP447
|
4.6
|
18.0
|
1.0
|
C
|
B:GLY446
|
4.6
|
19.8
|
1.0
|
CZ
|
B:PHE496
|
4.6
|
23.8
|
1.0
|
N
|
B:ASN475
|
4.7
|
22.1
|
1.0
|
C
|
B:TYR477
|
4.9
|
21.8
|
1.0
|
CA
|
B:ASP474
|
4.9
|
23.2
|
1.0
|
C
|
B:ASP447
|
4.9
|
19.3
|
1.0
|
CB
|
B:ASN478
|
4.9
|
21.2
|
1.0
|
C
|
B:ASP474
|
5.0
|
22.0
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1ozh
Go back to
Magnesium Binding Sites List in 1ozh
Magnesium binding site 3 out
of 4 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1422
b:19.7
occ:1.00
|
OD1
|
C:ASP474
|
2.0
|
19.4
|
1.0
|
O
|
C:GLY476
|
2.0
|
20.2
|
1.0
|
O
|
C:HOH1451
|
2.1
|
18.7
|
1.0
|
O2A
|
C:HE31423
|
2.1
|
18.5
|
1.0
|
O3B
|
C:HE31423
|
2.1
|
17.5
|
1.0
|
OD1
|
C:ASP447
|
2.2
|
21.2
|
1.0
|
CG
|
C:ASP474
|
3.1
|
23.6
|
1.0
|
PB
|
C:HE31423
|
3.2
|
20.0
|
1.0
|
PA
|
C:HE31423
|
3.2
|
20.9
|
1.0
|
C
|
C:GLY476
|
3.2
|
20.2
|
1.0
|
CG
|
C:ASP447
|
3.3
|
23.2
|
1.0
|
O1A
|
C:HE31423
|
3.3
|
17.3
|
1.0
|
OD2
|
C:ASP474
|
3.6
|
21.9
|
1.0
|
O1B
|
C:HE31423
|
3.6
|
20.1
|
1.0
|
O7
|
C:HE31423
|
3.7
|
20.8
|
1.0
|
OD2
|
C:ASP447
|
3.8
|
23.4
|
1.0
|
N
|
C:GLY476
|
3.8
|
21.5
|
1.0
|
N
|
C:ASP447
|
3.8
|
18.6
|
1.0
|
CA
|
C:GLY476
|
4.1
|
21.4
|
1.0
|
N
|
C:GLY448
|
4.1
|
20.7
|
1.0
|
N
|
C:ASN478
|
4.2
|
20.3
|
1.0
|
N
|
C:TYR477
|
4.2
|
19.7
|
1.0
|
CB
|
C:ASP474
|
4.3
|
20.6
|
1.0
|
CA
|
C:TYR477
|
4.3
|
19.2
|
1.0
|
N
|
C:ASP474
|
4.5
|
19.2
|
1.0
|
O2B
|
C:HE31423
|
4.5
|
20.5
|
1.0
|
O3A
|
C:HE31423
|
4.5
|
17.4
|
1.0
|
CB
|
C:ASP447
|
4.5
|
20.1
|
1.0
|
O
|
C:TRP472
|
4.5
|
21.8
|
1.0
|
CA
|
C:GLY446
|
4.6
|
18.6
|
1.0
|
CA
|
C:ASP447
|
4.6
|
18.5
|
1.0
|
CZ
|
C:PHE496
|
4.6
|
22.4
|
1.0
|
C
|
C:GLY446
|
4.6
|
18.6
|
1.0
|
N
|
C:ASN475
|
4.7
|
21.4
|
1.0
|
C
|
C:TYR477
|
4.8
|
19.7
|
1.0
|
CA
|
C:ASP474
|
4.8
|
20.6
|
1.0
|
C
|
C:ASP447
|
4.9
|
19.6
|
1.0
|
CB
|
C:ASN478
|
5.0
|
18.4
|
1.0
|
C
|
C:ASP474
|
5.0
|
21.0
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1ozh
Go back to
Magnesium Binding Sites List in 1ozh
Magnesium binding site 4 out
of 4 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate.
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1432
b:32.1
occ:1.00
|
OD1
|
D:ASP474
|
2.0
|
30.8
|
1.0
|
O
|
D:GLY476
|
2.0
|
26.2
|
1.0
|
OD1
|
D:ASP447
|
2.1
|
23.9
|
1.0
|
O3B
|
D:HE31433
|
2.1
|
25.0
|
1.0
|
O2A
|
D:HE31433
|
2.1
|
27.0
|
1.0
|
O
|
D:HOH1473
|
2.2
|
28.7
|
1.0
|
CG
|
D:ASP474
|
3.0
|
31.3
|
1.0
|
PB
|
D:HE31433
|
3.1
|
25.2
|
1.0
|
PA
|
D:HE31433
|
3.1
|
25.1
|
1.0
|
CG
|
D:ASP447
|
3.2
|
25.7
|
1.0
|
C
|
D:GLY476
|
3.2
|
26.6
|
1.0
|
OD2
|
D:ASP474
|
3.3
|
31.4
|
1.0
|
O1A
|
D:HE31433
|
3.3
|
27.2
|
1.0
|
O1B
|
D:HE31433
|
3.6
|
26.6
|
1.0
|
O7
|
D:HE31433
|
3.7
|
23.5
|
1.0
|
OD2
|
D:ASP447
|
3.7
|
26.6
|
1.0
|
N
|
D:ASP447
|
3.8
|
24.0
|
1.0
|
N
|
D:GLY476
|
3.9
|
26.5
|
1.0
|
CA
|
D:GLY476
|
4.1
|
26.4
|
1.0
|
N
|
D:ASN478
|
4.2
|
29.1
|
1.0
|
N
|
D:TYR477
|
4.2
|
25.4
|
1.0
|
N
|
D:GLY448
|
4.2
|
24.7
|
1.0
|
CB
|
D:ASP474
|
4.3
|
28.2
|
1.0
|
CA
|
D:TYR477
|
4.3
|
25.6
|
1.0
|
O2B
|
D:HE31433
|
4.4
|
26.9
|
1.0
|
CB
|
D:ASP447
|
4.4
|
23.7
|
1.0
|
O3A
|
D:HE31433
|
4.5
|
26.0
|
1.0
|
CZ
|
D:PHE496
|
4.5
|
25.0
|
1.0
|
CA
|
D:GLY446
|
4.5
|
24.4
|
1.0
|
O
|
D:TRP472
|
4.5
|
26.5
|
1.0
|
CA
|
D:ASP447
|
4.6
|
24.5
|
1.0
|
C
|
D:GLY446
|
4.6
|
23.0
|
1.0
|
N
|
D:ASP474
|
4.6
|
27.3
|
1.0
|
N
|
D:ASN475
|
4.7
|
28.4
|
1.0
|
C
|
D:TYR477
|
4.8
|
27.4
|
1.0
|
CA
|
D:ASP474
|
4.9
|
28.2
|
1.0
|
C
|
D:ASP447
|
4.9
|
24.4
|
1.0
|
CB
|
D:ASN478
|
4.9
|
30.7
|
1.0
|
C7
|
D:HE31433
|
4.9
|
27.3
|
1.0
|
C
|
D:ASP474
|
5.0
|
28.3
|
1.0
|
|
Reference:
S.S.Pang,
R.G.Duggleby,
R.L.Schowen,
L.W.Guddat.
The Crystal Structures of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate. J.Biol.Chem. V. 279 2242 2004.
ISSN: ISSN 0021-9258
PubMed: 14557277
DOI: 10.1074/JBC.M304038200
Page generated: Tue Aug 13 10:46:13 2024
|