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Arsenic in PDB 2e11: The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site

Protein crystallography data

The structure of The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site, PDB code: 2e11 was solved by K.-H.Chin, Y.-D.Tsai, N.-L.Chan, K.-F.Huang, A.H.-J.Wang, S.-H.Chou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 104.83 / 1.73
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 143.280, 154.305, 51.158, 90.00, 90.00, 90.00
R / Rfree (%) 14 / 21.7

Arsenic Binding Sites:

The binding sites of Arsenic atom in the The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site (pdb code 2e11). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 4 binding sites of Arsenic where determined in the The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site, PDB code: 2e11:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in 2e11

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Arsenic binding site 1 out of 4 in the The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As1266

b:25.6
occ:1.00
AS A:CAC1266 0.0 25.6 1.0
O2 A:CAC1266 1.8 27.2 1.0
C1 A:CAC1266 2.0 23.5 1.0
C2 A:CAC1266 2.0 24.7 1.0
SG A:CYS143 2.2 13.3 1.0
CB A:CYS143 3.1 12.3 1.0
N A:TYR144 3.7 10.3 1.0
NZ A:LYS109 3.8 13.8 1.0
O A:ASN174 3.9 11.3 1.0
OE2 A:GLU43 3.9 15.5 1.0
CG A:PHE113 4.1 9.3 1.0
CD2 A:PHE113 4.2 11.2 1.0
CA A:CYS143 4.3 11.1 1.0
CB A:PHE113 4.3 10.5 1.0
CB A:TYR144 4.3 10.4 1.0
C A:CYS143 4.3 10.6 1.0
CA A:TYR144 4.4 9.8 1.0
CD1 A:PHE113 4.4 11.8 1.0
OE1 A:GLU43 4.5 13.5 1.0
C A:ASN174 4.6 10.8 1.0
CD A:GLU43 4.6 11.6 1.0
CE2 A:PHE113 4.7 11.3 1.0
N A:ASN174 4.9 12.6 1.0
CE1 A:PHE113 4.9 11.2 1.0
CZ A:PHE49 4.9 13.9 1.0
CE A:LYS109 4.9 12.6 1.0
CE3 A:TRP175 5.0 8.3 1.0

Arsenic binding site 2 out of 4 in 2e11

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Arsenic binding site 2 out of 4 in the The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As1266

b:26.7
occ:1.00
AS B:CAC1266 0.0 26.7 1.0
O2 B:CAC1266 1.8 27.0 1.0
C1 B:CAC1266 2.0 24.3 1.0
C2 B:CAC1266 2.0 24.9 1.0
SG B:CYS143 2.2 12.6 1.0
CB B:CYS143 3.1 10.2 1.0
N B:TYR144 3.7 9.8 1.0
O B:ASN174 3.9 9.9 1.0
NZ B:LYS109 3.9 11.7 1.0
OE2 B:GLU43 3.9 15.1 1.0
CG B:PHE113 4.0 9.7 1.0
CB B:PHE113 4.2 10.0 1.0
CD2 B:PHE113 4.2 11.2 1.0
CB B:TYR144 4.2 8.3 1.0
CA B:CYS143 4.3 9.9 1.0
C B:CYS143 4.3 9.8 1.0
CD1 B:PHE113 4.4 11.3 1.0
CA B:TYR144 4.4 8.6 1.0
OE1 B:GLU43 4.5 11.9 1.0
C B:ASN174 4.6 10.2 1.0
CD B:GLU43 4.6 13.1 1.0
O B:HOH1429 4.7 21.3 1.0
CE2 B:PHE113 4.7 12.9 1.0
CE1 B:PHE113 4.8 11.6 1.0
CE B:LYS109 4.9 12.2 1.0
CZ B:PHE49 4.9 15.2 1.0
CE2 B:PHE49 4.9 14.4 1.0
N B:ASN174 4.9 10.4 1.0
CZ B:PHE113 5.0 11.2 1.0

Arsenic binding site 3 out of 4 in 2e11

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Arsenic binding site 3 out of 4 in the The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
C:As1266

b:30.7
occ:1.00
AS C:CAC1266 0.0 30.7 1.0
O2 C:CAC1266 1.7 33.2 1.0
C2 C:CAC1266 2.0 29.6 1.0
C1 C:CAC1266 2.0 29.5 1.0
SG C:CYS143 2.2 15.1 1.0
CB C:CYS143 3.1 12.3 1.0
N C:TYR144 3.7 10.3 1.0
O C:ASN174 3.9 11.6 1.0
NZ C:LYS109 3.9 15.6 1.0
OE2 C:GLU43 4.0 15.8 1.0
CG C:PHE113 4.0 18.8 1.0
CD1 C:PHE113 4.2 20.4 1.0
CB C:PHE113 4.3 18.2 1.0
CD2 C:PHE113 4.3 20.5 1.0
CA C:CYS143 4.3 11.4 1.0
CB C:TYR144 4.3 10.1 1.0
C C:CYS143 4.3 11.0 1.0
CA C:TYR144 4.4 9.4 1.0
OE1 C:GLU43 4.5 14.9 1.0
O C:HOH1278 4.6 22.5 1.0
C C:ASN174 4.6 11.6 1.0
CD C:GLU43 4.7 13.3 1.0
CE1 C:PHE113 4.7 20.2 1.0
CE2 C:PHE113 4.7 20.9 1.0
N C:ASN174 4.8 12.2 1.0
CZ C:PHE113 4.9 20.2 1.0
CE C:LYS109 4.9 16.5 1.0
CE3 C:TRP175 4.9 8.4 1.0
CZ C:PHE49 5.0 22.9 1.0

Arsenic binding site 4 out of 4 in 2e11

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Arsenic binding site 4 out of 4 in the The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of The Crystal Structure of XC1258 From Xanthomonas Campestris: A Cn- Hydrolase Superfamily Protein with An Arsenic Adduct in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
D:As1266

b:31.8
occ:1.00
AS D:CAC1266 0.0 31.8 1.0
O2 D:CAC1266 1.8 30.8 1.0
C2 D:CAC1266 2.0 31.4 1.0
C1 D:CAC1266 2.0 30.5 1.0
SG D:CYS143 2.3 15.5 1.0
CB D:CYS143 3.1 13.1 1.0
N D:TYR144 3.7 10.2 1.0
O D:ASN174 3.9 12.1 1.0
NZ D:LYS109 4.0 15.7 1.0
OE2 D:GLU43 4.0 16.3 1.0
CG D:PHE113 4.1 17.4 1.0
CD2 D:PHE113 4.2 17.8 1.0
CB D:PHE113 4.3 16.4 1.0
CA D:CYS143 4.3 12.1 1.0
CB D:TYR144 4.3 10.3 1.0
CD1 D:PHE113 4.4 18.3 1.0
C D:CYS143 4.4 11.4 1.0
OE1 D:GLU43 4.4 15.1 1.0
CA D:TYR144 4.4 9.3 1.0
C D:ASN174 4.6 11.8 1.0
CD D:GLU43 4.6 12.5 1.0
CE2 D:PHE113 4.7 18.4 1.0
N D:ASN174 4.8 11.7 1.0
CE1 D:PHE113 4.8 19.5 1.0
CZ D:PHE49 4.9 23.4 1.0
CE3 D:TRP175 5.0 9.2 1.0
CE2 D:PHE49 5.0 24.5 1.0
CE D:LYS109 5.0 13.6 1.0
CZ D:PHE113 5.0 18.4 1.0

Reference:

K.-H.Chin, Y.-D.Tsai, N.-L.Chan, K.-F.Huang, A.H.-J.Wang, S.-H.Chou. The Crystal Structure of XC1258 From Xanthomonas Campestris: A Putative Procaryotic Nit Protein with An Arsenic Adduct in the Active Site Proteins V. 69 665 2007.
ISSN: ISSN 0887-3585
PubMed: 17640068
DOI: 10.1002/PROT.21501
Page generated: Tue Oct 27 16:48:48 2020

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