Magnesium in PDB 5hmm: Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
Enzymatic activity of Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
All present enzymatic activity of Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions:
3.1.11.3;
Protein crystallography data
The structure of Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions, PDB code: 5hmm
was solved by
C.S.Flemming,
S.E.Sedelnikova,
J.B.Rafferty,
J.R.Sayers,
P.J.Artymiuk,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
38.35 /
1.50
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
46.831,
58.591,
59.729,
66.88,
79.40,
73.78
|
R / Rfree (%)
|
14.8 /
19.7
|
Other elements in 5hmm:
The structure of Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
(pdb code 5hmm). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the
Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions, PDB code: 5hmm:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
Magnesium binding site 1 out
of 6 in 5hmm
Go back to
Magnesium Binding Sites List in 5hmm
Magnesium binding site 1 out
of 6 in the Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
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 T5 D15 Protein Co-Crystallized with Metal Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg302
b:10.0
occ:1.00
|
O
|
A:HOH524
|
2.0
|
10.8
|
1.0
|
O
|
A:HOH642
|
2.0
|
11.4
|
1.0
|
O
|
A:HOH440
|
2.1
|
10.2
|
1.0
|
O
|
A:HOH425
|
2.1
|
12.8
|
1.0
|
O
|
A:HOH438
|
2.1
|
11.8
|
1.0
|
OD1
|
A:ASP130
|
2.2
|
9.0
|
1.0
|
CG
|
A:ASP130
|
3.2
|
9.0
|
1.0
|
OD2
|
A:ASP130
|
3.5
|
15.4
|
1.0
|
MG
|
A:MG303
|
3.6
|
32.4
|
1.0
|
OD2
|
A:ASP153
|
3.9
|
20.9
|
1.0
|
OE2
|
A:GLU128
|
4.0
|
20.3
|
1.0
|
O
|
A:HOH575
|
4.1
|
34.4
|
1.0
|
OD2
|
A:ASP68
|
4.2
|
10.9
|
1.0
|
OD1
|
A:ASP68
|
4.2
|
11.6
|
1.0
|
NE1
|
A:TRP156
|
4.3
|
10.5
|
1.0
|
OD2
|
A:ASP26
|
4.3
|
8.3
|
1.0
|
O
|
A:HOH510
|
4.3
|
31.3
|
1.0
|
OD1
|
A:ASP26
|
4.4
|
11.5
|
1.0
|
N
|
A:ASP130
|
4.5
|
7.1
|
1.0
|
CB
|
A:ASP130
|
4.5
|
8.8
|
1.0
|
CG
|
A:ASP68
|
4.6
|
12.9
|
1.0
|
O
|
A:HOH608
|
4.7
|
32.2
|
1.0
|
CG
|
A:ASP26
|
4.8
|
7.7
|
1.0
|
CA
|
A:ASP130
|
4.9
|
8.0
|
1.0
|
CG
|
A:ASP153
|
5.0
|
16.0
|
1.0
|
|
Magnesium binding site 2 out
of 6 in 5hmm
Go back to
Magnesium Binding Sites List in 5hmm
Magnesium binding site 2 out
of 6 in the Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
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 T5 D15 Protein Co-Crystallized with Metal Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg303
b:32.4
occ:1.00
|
O
|
A:HOH524
|
1.9
|
10.8
|
1.0
|
OD2
|
A:ASP130
|
2.2
|
15.4
|
1.0
|
OD2
|
A:ASP153
|
2.4
|
20.9
|
1.0
|
OD2
|
A:ASP155
|
2.5
|
29.6
|
1.0
|
CG
|
A:ASP130
|
3.3
|
9.0
|
1.0
|
CG
|
A:ASP155
|
3.4
|
31.5
|
1.0
|
CG
|
A:ASP153
|
3.5
|
16.0
|
1.0
|
O
|
A:HOH592
|
3.5
|
33.0
|
1.0
|
O
|
A:HOH454
|
3.5
|
30.6
|
1.0
|
MG
|
A:MG302
|
3.6
|
10.0
|
1.0
|
OD1
|
A:ASP130
|
3.6
|
9.0
|
1.0
|
CB
|
A:ASP155
|
3.6
|
26.5
|
1.0
|
O
|
A:HOH438
|
3.7
|
11.8
|
1.0
|
O
|
A:HOH401
|
3.8
|
44.0
|
1.0
|
OD1
|
A:ASP153
|
3.9
|
14.7
|
1.0
|
O
|
A:HOH575
|
4.3
|
34.4
|
1.0
|
OE2
|
A:GLU128
|
4.3
|
20.3
|
1.0
|
O
|
A:HOH642
|
4.5
|
11.4
|
1.0
|
OD1
|
A:ASP155
|
4.5
|
32.1
|
1.0
|
CB
|
A:ASP130
|
4.5
|
8.8
|
1.0
|
O
|
A:HOH425
|
4.6
|
12.8
|
1.0
|
NE1
|
A:TRP156
|
4.7
|
10.5
|
1.0
|
CD1
|
A:TRP156
|
4.7
|
10.0
|
1.0
|
O
|
A:HOH418
|
4.7
|
38.5
|
1.0
|
CB
|
A:ASP153
|
4.8
|
11.8
|
1.0
|
OD2
|
A:ASP204
|
4.8
|
34.1
|
1.0
|
|
Magnesium binding site 3 out
of 6 in 5hmm
Go back to
Magnesium Binding Sites List in 5hmm
Magnesium binding site 3 out
of 6 in the Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
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 T5 D15 Protein Co-Crystallized with Metal Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg304
b:33.1
occ:0.70
|
O
|
A:HOH401
|
2.0
|
44.0
|
1.0
|
O
|
A:HOH418
|
2.1
|
38.5
|
1.0
|
O
|
A:HOH556
|
2.2
|
34.4
|
1.0
|
OD2
|
A:ASP201
|
2.3
|
40.1
|
1.0
|
O
|
A:HOH532
|
2.5
|
37.8
|
1.0
|
OD1
|
A:ASP155
|
2.7
|
32.1
|
1.0
|
CG
|
A:ASP201
|
3.3
|
32.8
|
1.0
|
CG
|
A:ASP155
|
3.4
|
31.5
|
1.0
|
OD2
|
A:ASP155
|
3.5
|
29.6
|
1.0
|
OD1
|
A:ASP201
|
3.6
|
27.4
|
1.0
|
O
|
A:HOH403
|
3.8
|
39.2
|
1.0
|
OD2
|
A:ASP204
|
4.0
|
34.1
|
1.0
|
O
|
A:HOH560
|
4.2
|
38.4
|
1.0
|
OD1
|
A:ASP153
|
4.3
|
14.7
|
1.0
|
CB
|
A:ASP201
|
4.6
|
22.9
|
1.0
|
CB
|
A:ASP155
|
4.7
|
26.5
|
1.0
|
CG
|
A:ASP204
|
4.8
|
24.9
|
1.0
|
|
Magnesium binding site 4 out
of 6 in 5hmm
Go back to
Magnesium Binding Sites List in 5hmm
Magnesium binding site 4 out
of 6 in the Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
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 T5 D15 Protein Co-Crystallized with Metal Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg301
b:7.0
occ:1.00
|
O
|
B:HOH429
|
2.0
|
7.0
|
1.0
|
O
|
B:HOH438
|
2.0
|
7.8
|
1.0
|
O
|
B:HOH676
|
2.1
|
10.7
|
1.0
|
O
|
B:HOH462
|
2.1
|
10.9
|
1.0
|
O
|
B:HOH412
|
2.1
|
7.5
|
1.0
|
OD1
|
B:ASP130
|
2.2
|
8.2
|
1.0
|
CG
|
B:ASP130
|
3.2
|
9.3
|
1.0
|
OD2
|
B:ASP130
|
3.5
|
13.2
|
1.0
|
OD2
|
B:ASP153
|
3.9
|
18.6
|
1.0
|
NE1
|
B:TRP156
|
4.1
|
9.5
|
1.0
|
O
|
B:HOH435
|
4.1
|
32.4
|
1.0
|
OD2
|
B:ASP68
|
4.1
|
13.0
|
1.0
|
OE2
|
B:GLU128
|
4.2
|
22.2
|
1.0
|
OD1
|
B:ASP68
|
4.3
|
13.1
|
1.0
|
OD2
|
B:ASP26
|
4.3
|
7.5
|
1.0
|
OD1
|
B:ASP26
|
4.3
|
9.0
|
1.0
|
O
|
B:HOH537
|
4.5
|
39.9
|
1.0
|
CB
|
B:ASP130
|
4.5
|
8.4
|
1.0
|
N
|
B:ASP130
|
4.5
|
7.1
|
1.0
|
NZ
|
B:LYS83
|
4.6
|
21.1
|
1.0
|
CG
|
B:ASP68
|
4.6
|
11.0
|
1.0
|
O
|
B:HOH405
|
4.6
|
32.5
|
1.0
|
CG
|
B:ASP26
|
4.8
|
6.8
|
1.0
|
O
|
B:HOH649
|
4.8
|
18.8
|
1.0
|
CD1
|
B:TRP156
|
4.9
|
9.2
|
1.0
|
CA
|
B:ASP130
|
5.0
|
8.0
|
1.0
|
|
Magnesium binding site 5 out
of 6 in 5hmm
Go back to
Magnesium Binding Sites List in 5hmm
Magnesium binding site 5 out
of 6 in the Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
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 T5 D15 Protein Co-Crystallized with Metal Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg302
b:45.3
occ:1.00
|
O
|
B:HOH682
|
1.9
|
33.4
|
1.0
|
O
|
B:HOH449
|
2.1
|
51.4
|
1.0
|
O
|
B:HOH452
|
2.2
|
35.7
|
1.0
|
OD2
|
B:ASP201
|
2.2
|
26.2
|
1.0
|
O
|
B:HOH506
|
2.4
|
49.9
|
1.0
|
O
|
B:HOH604
|
2.9
|
45.0
|
1.0
|
CG
|
B:ASP201
|
3.2
|
18.3
|
1.0
|
OD1
|
B:ASP201
|
3.4
|
15.0
|
1.0
|
O
|
A:HOH404
|
3.6
|
31.9
|
1.0
|
OD2
|
B:ASP204
|
4.1
|
37.3
|
1.0
|
OD1
|
B:ASP155
|
4.3
|
19.7
|
1.0
|
O
|
A:HOH489
|
4.3
|
22.7
|
1.0
|
O
|
B:HOH573
|
4.4
|
32.5
|
1.0
|
CB
|
B:ASP201
|
4.6
|
13.8
|
1.0
|
CE
|
B:LYS196
|
4.6
|
15.7
|
0.5
|
CG
|
B:ASP204
|
4.6
|
22.8
|
1.0
|
O
|
B:HOH634
|
4.6
|
52.1
|
1.0
|
OD2
|
B:ASP155
|
4.7
|
33.5
|
1.0
|
OD1
|
B:ASP204
|
4.8
|
26.6
|
1.0
|
CG
|
B:ASP155
|
4.9
|
22.0
|
1.0
|
O
|
B:HOH571
|
4.9
|
16.8
|
1.0
|
|
Magnesium binding site 6 out
of 6 in 5hmm
Go back to
Magnesium Binding Sites List in 5hmm
Magnesium binding site 6 out
of 6 in the Crystal Structure of T5 D15 Protein Co-Crystallized with Metal Ions
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 T5 D15 Protein Co-Crystallized with Metal Ions within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg303
b:19.1
occ:1.00
|
O
|
B:HOH600
|
2.0
|
20.2
|
1.0
|
O
|
B:HOH401
|
2.0
|
22.8
|
1.0
|
O
|
B:HOH443
|
2.1
|
19.4
|
1.0
|
O
|
B:HOH594
|
2.1
|
20.5
|
1.0
|
O
|
B:HOH418
|
2.1
|
22.5
|
1.0
|
OD1
|
B:ASP87
|
2.2
|
15.1
|
1.0
|
CG
|
B:ASP87
|
3.2
|
16.7
|
1.0
|
OD2
|
B:ASP87
|
3.5
|
17.4
|
1.0
|
OE1
|
B:GLU88
|
4.1
|
27.2
|
1.0
|
OD1
|
B:ASN85
|
4.1
|
18.9
|
1.0
|
O
|
B:HOH723
|
4.2
|
29.7
|
1.0
|
N
|
B:GLU88
|
4.4
|
12.7
|
1.0
|
CB
|
B:ASP87
|
4.5
|
13.9
|
1.0
|
OE2
|
B:GLU81
|
4.5
|
41.4
|
1.0
|
N
|
B:ASP87
|
4.5
|
14.1
|
1.0
|
O
|
B:HOH408
|
4.6
|
7.3
|
1.0
|
OE1
|
B:GLU81
|
4.6
|
32.5
|
1.0
|
CA
|
B:ASP87
|
4.8
|
15.2
|
1.0
|
CD
|
B:GLU81
|
4.9
|
33.7
|
1.0
|
C
|
B:ASP87
|
4.9
|
12.4
|
1.0
|
|
Reference:
F.A.Almalki,
C.S.Flemming,
J.Zhang,
M.Feng,
S.E.Sedelnikova,
T.Ceska,
J.B.Rafferty,
J.R.Sayers,
P.J.Artymiuk.
Direct Observation of Dna Threading in Flap Endonuclease Complexes. Nat.Struct.Mol.Biol. V. 23 640 2016.
ISSN: ESSN 1545-9985
PubMed: 27273516
DOI: 10.1038/NSMB.3241
Page generated: Sun Sep 29 16:01:31 2024
|