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Arsenic in PDB 2vqh: Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II)

Protein crystallography data

The structure of Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II), PDB code: 2vqh was solved by K.Ziegler, R.Benz, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.53 / 2.89
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 81.457, 81.457, 163.346, 90.00, 90.00, 120.00
R / Rfree (%) 24.7 / 25.6

Other elements in 2vqh:

The structure of Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II) also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II) (pdb code 2vqh). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 3 binding sites of Arsenic where determined in the Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II), PDB code: 2vqh:
Jump to Arsenic binding site number: 1; 2; 3;

Arsenic binding site 1 out of 3 in 2vqh

Go back to Arsenic Binding Sites List in 2vqh
Arsenic binding site 1 out of 3 in the Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II)


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1094

b:78.6
occ:1.00
AS A:CAC1094 0.0 78.6 1.0
O1 A:CAC1094 1.7 78.6 1.0
O2 A:CAC1094 1.7 77.8 1.0
C1 A:CAC1094 2.0 77.6 1.0
C2 A:CAC1094 2.0 77.3 1.0
ZN A:ZN1092 3.1 70.3 1.0
ZN A:ZN1093 3.1 80.6 1.0
NZ A:LYS30 3.7 70.0 1.0
O2 A:CAC1095 4.2 76.6 1.0
O1 A:CAC1095 4.2 77.7 1.0
OE1 A:GLU37 4.3 84.1 1.0
OE2 A:GLU26 4.5 67.4 1.0
CE A:LYS30 4.6 67.2 1.0
AS A:CAC1095 4.7 76.2 1.0
OE2 A:GLU37 4.7 85.2 1.0
CD A:GLU37 5.0 84.5 1.0
C2 A:CAC1095 5.0 75.8 1.0

Arsenic binding site 2 out of 3 in 2vqh

Go back to Arsenic Binding Sites List in 2vqh
Arsenic binding site 2 out of 3 in the Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II)


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1095

b:76.2
occ:1.00
AS A:CAC1095 0.0 76.2 1.0
O1 A:CAC1095 1.7 77.7 1.0
O2 A:CAC1095 1.7 76.6 1.0
C1 A:CAC1095 2.0 75.6 1.0
C2 A:CAC1095 2.0 75.8 1.0
ZN A:ZN1092 3.1 70.3 1.0
ZN A:ZN1093 3.2 80.6 1.0
O1 A:CAC1094 3.8 78.6 1.0
OE2 A:GLU26 4.1 67.4 1.0
O2 A:CAC1094 4.3 77.8 1.0
O A:LEU83 4.4 63.7 1.0
OE2 A:GLU37 4.4 85.2 1.0
AS A:CAC1094 4.7 78.6 1.0
CD A:GLU26 4.9 66.1 1.0
O A:GLY82 4.9 68.5 1.0
OE1 A:GLU37 5.0 84.1 1.0
CD A:GLU37 5.0 84.5 1.0

Arsenic binding site 3 out of 3 in 2vqh

Go back to Arsenic Binding Sites List in 2vqh
Arsenic binding site 3 out of 3 in the Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II)


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Crystal Structure of Porb From Corynebacterium Glutamicum ( Crystal Form II) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As1092

b:91.9
occ:1.00
AS B:CAC1092 0.0 91.9 1.0
O2 B:CAC1092 1.7 92.8 1.0
O1 B:CAC1092 1.7 91.1 1.0
C1 B:CAC1092 2.0 92.3 1.0
C2 B:CAC1092 2.0 92.2 1.0
ZN A:ZN1091 3.0 83.7 1.0
ZN B:ZN1090 3.2 97.9 1.0
OD2 A:ASP76 4.0 70.8 1.0
OD1 A:ASP76 4.1 66.8 1.0
OD1 B:ASP76 4.1 72.9 1.0
ND2 B:ASN41 4.3 66.7 1.0
OD2 A:ASP87 4.4 85.6 1.0
CG A:ASP76 4.4 67.3 1.0
OD2 B:ASP76 4.5 77.2 1.0
CG B:ASN41 4.6 67.4 1.0
CG B:ASP76 4.6 73.1 1.0
OD2 B:ASP87 4.6 80.0 1.0
OD1 B:ASN41 4.7 66.0 1.0
ND2 A:ASN41 4.9 62.0 1.0

Reference:

K.Ziegler, R.Benz, G.E.Schulz. A Putative Alpha-Helical Porin From Corynebacterium Glutamicum. J.Mol.Biol. V. 379 482 2008.
ISSN: ISSN 0022-2836
PubMed: 18462756
DOI: 10.1016/J.JMB.2008.04.017
Page generated: Wed Jul 10 11:30:57 2024

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