Zinc in PDB 2y3g: Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs
Protein crystallography data
The structure of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs, PDB code: 2y3g
was solved by
J.Trepreau,
E.Girard,
A.P.Maillard,
E.De Rosny,
I.Petit-Haertlein,
R.Kahn,
J.Coves,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.666 /
1.91
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
31.896,
81.809,
93.336,
90.00,
90.47,
90.00
|
R / Rfree (%)
|
18.73 /
23.82
|
Other elements in 2y3g:
The structure of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs
(pdb code 2y3g). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs, PDB code: 2y3g:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 2y3g
Go back to
Zinc Binding Sites List in 2y3g
Zinc binding site 1 out
of 3 in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn150
b:40.7
occ:0.60
|
NE2
|
A:HIS46
|
2.0
|
69.1
|
0.6
|
OE1
|
A:GLU63
|
2.2
|
35.9
|
1.0
|
NE2
|
A:HIS42
|
2.3
|
71.0
|
1.0
|
NE2
|
A:HIS119
|
2.5
|
32.5
|
1.0
|
OE2
|
A:GLU63
|
2.5
|
40.8
|
1.0
|
CE1
|
A:HIS46
|
2.6
|
68.3
|
0.6
|
CD
|
A:GLU63
|
2.7
|
45.9
|
1.0
|
CD2
|
A:HIS42
|
2.7
|
67.5
|
1.0
|
CD2
|
A:HIS46
|
3.1
|
65.9
|
0.6
|
CD2
|
A:HIS119
|
3.1
|
32.1
|
1.0
|
CE1
|
A:HIS42
|
3.5
|
73.2
|
1.0
|
CE1
|
A:HIS119
|
3.6
|
27.4
|
1.0
|
ND1
|
A:HIS46
|
3.7
|
65.3
|
0.6
|
SE
|
A:MSE123
|
3.8
|
47.6
|
0.8
|
CG
|
A:HIS46
|
4.0
|
65.7
|
0.6
|
CE
|
A:MSE123
|
4.0
|
6.8
|
0.2
|
CG
|
A:HIS42
|
4.0
|
67.1
|
1.0
|
CG
|
A:GLU63
|
4.2
|
33.5
|
1.0
|
CD2
|
A:PHE66
|
4.2
|
29.1
|
1.0
|
CE
|
A:MSE123
|
4.3
|
14.5
|
0.8
|
ND1
|
A:HIS42
|
4.4
|
69.9
|
1.0
|
CG
|
A:HIS119
|
4.4
|
25.1
|
1.0
|
CE2
|
A:PHE66
|
4.6
|
37.8
|
1.0
|
ND1
|
A:HIS119
|
4.6
|
31.1
|
1.0
|
CB
|
A:GLU63
|
4.9
|
28.0
|
1.0
|
CG
|
A:MSE123
|
4.9
|
27.8
|
0.2
|
O
|
A:HIS42
|
4.9
|
54.2
|
1.0
|
ND1
|
A:HIS46
|
5.0
|
68.0
|
0.4
|
CG
|
A:MSE123
|
5.0
|
29.7
|
0.8
|
|
Zinc binding site 2 out
of 3 in 2y3g
Go back to
Zinc Binding Sites List in 2y3g
Zinc binding site 2 out
of 3 in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn150
b:36.4
occ:0.40
|
OE2
|
B:GLU63
|
2.1
|
48.6
|
1.0
|
NE2
|
B:HIS42
|
2.1
|
67.5
|
1.0
|
NE2
|
B:HIS46
|
2.1
|
29.2
|
0.4
|
NE2
|
B:HIS119
|
2.3
|
29.1
|
1.0
|
CD2
|
B:HIS42
|
2.5
|
70.9
|
1.0
|
CD
|
B:GLU63
|
2.7
|
55.0
|
1.0
|
OE1
|
B:GLU63
|
2.7
|
51.7
|
1.0
|
CD2
|
B:HIS46
|
2.8
|
32.3
|
0.4
|
CD2
|
B:HIS119
|
3.0
|
31.2
|
1.0
|
CE1
|
B:HIS46
|
3.3
|
34.6
|
0.4
|
CE1
|
B:HIS42
|
3.3
|
65.2
|
1.0
|
CE1
|
B:HIS119
|
3.5
|
31.8
|
1.0
|
SE
|
B:MSE123
|
3.6
|
37.9
|
0.5
|
CG
|
B:HIS42
|
3.8
|
66.3
|
1.0
|
SE
|
B:MSE123
|
4.0
|
40.5
|
0.3
|
CE
|
B:MSE123
|
4.0
|
21.1
|
0.5
|
CG
|
B:HIS46
|
4.1
|
39.2
|
0.4
|
CG
|
B:GLU63
|
4.1
|
51.4
|
1.0
|
ND1
|
B:HIS42
|
4.2
|
64.1
|
1.0
|
CD2
|
B:PHE66
|
4.2
|
30.9
|
1.0
|
CG
|
B:HIS119
|
4.2
|
26.8
|
1.0
|
ND1
|
B:HIS46
|
4.3
|
33.1
|
0.4
|
CE
|
B:MSE123
|
4.3
|
12.2
|
0.2
|
ND1
|
B:HIS119
|
4.4
|
25.7
|
1.0
|
CE2
|
B:PHE66
|
4.6
|
38.4
|
1.0
|
CG
|
B:MSE123
|
4.8
|
24.9
|
0.2
|
SE
|
B:MSE123
|
4.9
|
41.5
|
0.2
|
CG
|
B:MSE123
|
4.9
|
25.0
|
0.3
|
CG
|
B:MSE123
|
4.9
|
24.1
|
0.5
|
|
Zinc binding site 3 out
of 3 in 2y3g
Go back to
Zinc Binding Sites List in 2y3g
Zinc binding site 3 out
of 3 in the Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Se-Met Form of Cupriavidus Metallidurans CH34 Cnrxs within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn150
b:47.1
occ:0.25
|
OE1
|
C:GLU63
|
2.2
|
77.1
|
1.0
|
NE2
|
C:HIS42
|
2.4
|
58.6
|
1.0
|
NE2
|
C:HIS119
|
2.5
|
41.3
|
1.0
|
NE2
|
C:HIS46
|
2.5
|
70.4
|
0.6
|
SE
|
C:MSE123
|
2.7
|
61.6
|
0.6
|
CD
|
C:GLU63
|
2.8
|
80.2
|
1.0
|
CD2
|
C:HIS42
|
2.9
|
56.2
|
1.0
|
CD2
|
C:HIS119
|
3.2
|
35.2
|
1.0
|
CD2
|
C:HIS46
|
3.3
|
67.6
|
0.6
|
OE2
|
C:GLU63
|
3.3
|
86.5
|
1.0
|
CE1
|
C:HIS119
|
3.5
|
42.3
|
1.0
|
CE1
|
C:HIS46
|
3.5
|
73.2
|
0.6
|
CE1
|
C:HIS42
|
3.6
|
63.4
|
1.0
|
CG
|
C:GLU63
|
3.6
|
72.9
|
1.0
|
CG
|
C:MSE123
|
3.6
|
33.3
|
0.6
|
CG
|
C:MSE123
|
3.7
|
25.9
|
0.4
|
CE
|
C:MSE123
|
3.8
|
27.8
|
0.6
|
SE
|
C:MSE123
|
4.0
|
48.0
|
0.4
|
CG
|
C:HIS42
|
4.2
|
51.9
|
1.0
|
O
|
C:HOH2009
|
4.4
|
46.8
|
1.0
|
CG
|
C:HIS119
|
4.4
|
31.2
|
1.0
|
ND1
|
C:HIS42
|
4.5
|
59.8
|
1.0
|
CG
|
C:HIS46
|
4.5
|
67.7
|
0.6
|
ND1
|
C:HIS119
|
4.5
|
29.9
|
1.0
|
ND1
|
C:HIS46
|
4.6
|
72.5
|
0.6
|
CB
|
C:GLU63
|
4.7
|
62.4
|
1.0
|
CA
|
C:GLU63
|
4.9
|
46.4
|
1.0
|
CB
|
C:MSE123
|
4.9
|
30.6
|
0.4
|
CD2
|
C:PHE66
|
5.0
|
35.0
|
1.0
|
|
Reference:
J.Trepreau,
E.Girard,
A.P.Maillard,
E.De Rosny,
I.Petit-Haertlein,
R.Kahn,
J.Coves.
Structural Basis For Metal Sensing By Cnrx. J.Mol.Biol. V. 408 766 2011.
ISSN: ISSN 0022-2836
PubMed: 21414325
DOI: 10.1016/J.JMB.2011.03.014
Page generated: Thu Oct 17 05:42:48 2024
|