Zinc in PDB 7zvy: Thermococcus Kadokarensis Phosphomannose Isomerase
Protein crystallography data
The structure of Thermococcus Kadokarensis Phosphomannose Isomerase, PDB code: 7zvy
was solved by
F.Hoh,
A.Calio,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
64.79 /
2.16
|
Space group
|
P 31
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.158,
91.158,
113.378,
90,
90,
120
|
R / Rfree (%)
|
22.1 /
28.9
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Thermococcus Kadokarensis Phosphomannose Isomerase
(pdb code 7zvy). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Thermococcus Kadokarensis Phosphomannose Isomerase, PDB code: 7zvy:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 7zvy
Go back to
Zinc Binding Sites List in 7zvy
Zinc binding site 1 out
of 4 in the Thermococcus Kadokarensis Phosphomannose Isomerase
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Thermococcus Kadokarensis Phosphomannose Isomerase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn201
b:50.0
occ:1.00
|
OE1
|
A:GLU51
|
2.4
|
92.9
|
1.0
|
NE2
|
A:HIS46
|
2.4
|
90.8
|
1.0
|
NE2
|
A:HIS85
|
2.5
|
81.7
|
1.0
|
OE2
|
A:GLU51
|
2.6
|
73.5
|
1.0
|
CD
|
A:GLU51
|
2.8
|
84.0
|
1.0
|
CE1
|
A:HIS46
|
3.2
|
84.0
|
1.0
|
NE2
|
A:HIS44
|
3.2
|
69.4
|
1.0
|
CE1
|
A:HIS85
|
3.3
|
87.2
|
1.0
|
CD2
|
A:HIS46
|
3.6
|
77.1
|
1.0
|
CD2
|
A:HIS85
|
3.7
|
69.3
|
1.0
|
CD2
|
A:HIS44
|
3.7
|
74.7
|
1.0
|
CG
|
A:GLU51
|
4.2
|
68.0
|
1.0
|
CE1
|
A:HIS44
|
4.4
|
74.5
|
1.0
|
ND1
|
A:HIS46
|
4.4
|
100.9
|
1.0
|
ND1
|
A:HIS85
|
4.5
|
88.9
|
1.0
|
CG
|
A:HIS46
|
4.6
|
96.0
|
1.0
|
CZ
|
A:PHE53
|
4.7
|
64.8
|
1.0
|
CG
|
A:HIS85
|
4.7
|
68.9
|
1.0
|
CE1
|
A:PHE53
|
4.9
|
58.1
|
1.0
|
CB
|
A:GLU51
|
5.0
|
70.7
|
1.0
|
|
Zinc binding site 2 out
of 4 in 7zvy
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Zinc Binding Sites List in 7zvy
Zinc binding site 2 out
of 4 in the Thermococcus Kadokarensis Phosphomannose Isomerase
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Thermococcus Kadokarensis Phosphomannose Isomerase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn202
b:50.0
occ:1.00
|
CD1
|
A:PHE77
|
3.6
|
56.4
|
1.0
|
O
|
A:HOH311
|
3.6
|
64.6
|
1.0
|
CZ
|
G:PHE20
|
3.8
|
72.5
|
1.0
|
O
|
A:ILE76
|
3.9
|
69.6
|
1.0
|
CE1
|
A:PHE77
|
4.0
|
47.9
|
1.0
|
CE1
|
G:PHE20
|
4.4
|
79.2
|
1.0
|
CA
|
A:PHE77
|
4.5
|
53.8
|
1.0
|
CG
|
A:PHE77
|
4.6
|
49.4
|
1.0
|
CE2
|
G:PHE20
|
4.6
|
84.8
|
1.0
|
CE1
|
A:TYR69
|
4.7
|
60.1
|
1.0
|
OH
|
A:TYR69
|
4.8
|
60.5
|
1.0
|
CZ
|
A:TYR69
|
4.9
|
74.5
|
1.0
|
CB
|
A:PHE77
|
4.9
|
50.7
|
1.0
|
C
|
A:ILE76
|
5.0
|
47.8
|
1.0
|
|
Zinc binding site 3 out
of 4 in 7zvy
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Zinc Binding Sites List in 7zvy
Zinc binding site 3 out
of 4 in the Thermococcus Kadokarensis Phosphomannose Isomerase
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Thermococcus Kadokarensis Phosphomannose Isomerase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn201
b:50.0
occ:1.00
|
O
|
F:HOH307
|
2.2
|
62.5
|
1.0
|
OE1
|
F:GLU51
|
2.9
|
86.5
|
1.0
|
OE2
|
F:GLU51
|
3.0
|
72.6
|
1.0
|
NE2
|
F:HIS46
|
3.1
|
50.0
|
1.0
|
NE2
|
F:HIS44
|
3.1
|
79.3
|
1.0
|
CD
|
F:GLU51
|
3.3
|
84.8
|
1.0
|
CD2
|
F:HIS44
|
3.9
|
79.2
|
1.0
|
CD2
|
F:HIS46
|
4.1
|
50.0
|
1.0
|
CE1
|
F:HIS46
|
4.1
|
50.0
|
1.0
|
NE2
|
F:HIS85
|
4.1
|
81.6
|
1.0
|
CE1
|
F:HIS44
|
4.2
|
77.7
|
1.0
|
CD2
|
F:HIS85
|
4.4
|
81.2
|
1.0
|
CG
|
F:GLU51
|
4.7
|
66.5
|
1.0
|
CZ
|
F:PHE53
|
5.0
|
51.7
|
1.0
|
|
Zinc binding site 4 out
of 4 in 7zvy
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Zinc Binding Sites List in 7zvy
Zinc binding site 4 out
of 4 in the Thermococcus Kadokarensis Phosphomannose Isomerase
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Thermococcus Kadokarensis Phosphomannose Isomerase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Zn201
b:50.0
occ:1.00
|
CE1
|
G:HIS44
|
3.2
|
61.2
|
1.0
|
NE2
|
G:HIS44
|
3.4
|
56.7
|
1.0
|
OE1
|
G:GLU51
|
3.6
|
61.4
|
1.0
|
CD2
|
G:HIS85
|
3.6
|
58.5
|
1.0
|
OE2
|
G:GLU51
|
3.9
|
66.6
|
1.0
|
NE2
|
G:HIS85
|
4.1
|
62.0
|
1.0
|
CD
|
G:GLU51
|
4.2
|
65.5
|
1.0
|
CZ
|
G:PHE53
|
4.3
|
50.0
|
1.0
|
ND1
|
G:HIS44
|
4.5
|
60.7
|
1.0
|
CG1
|
G:VAL41
|
4.5
|
66.1
|
1.0
|
CD2
|
G:HIS44
|
4.8
|
56.7
|
1.0
|
CG
|
G:HIS85
|
4.9
|
52.8
|
1.0
|
|
Reference:
A.Calio,
C.Dubois,
S.Fontanay,
M.M.Koza,
F.Hoh,
C.Roumestand,
P.Oger,
J.Peters.
Unravelling the Adaptation Mechanisms to High Pressure in Proteins. Int J Mol Sci V. 23 2022.
ISSN: ESSN 1422-0067
PubMed: 35955607
DOI: 10.3390/IJMS23158469
Page generated: Wed Oct 30 17:20:43 2024
|