2E11
The Crystal Structure of XC1258 from Xanthomonas campestris: A CN-hydrolase Superfamily Protein with an Arsenic Adduct in the Active Site
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0050152 | molecular_function | omega-amidase activity |
A | 0106008 | molecular_function | 2-oxoglutaramate amidase activity |
B | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0050152 | molecular_function | omega-amidase activity |
B | 0106008 | molecular_function | 2-oxoglutaramate amidase activity |
C | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0050152 | molecular_function | omega-amidase activity |
C | 0106008 | molecular_function | 2-oxoglutaramate amidase activity |
D | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0050152 | molecular_function | omega-amidase activity |
D | 0106008 | molecular_function | 2-oxoglutaramate amidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CAC A 1266 |
Chain | Residue |
A | GLU43 |
A | PHE49 |
A | LYS109 |
A | PHE113 |
A | CYS143 |
A | TYR144 |
A | ASN174 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CAC B 1266 |
Chain | Residue |
B | LYS109 |
B | PHE113 |
B | CYS143 |
B | TYR144 |
B | ASN174 |
B | GLU43 |
B | PHE49 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CAC C 1266 |
Chain | Residue |
C | GLU43 |
C | PHE49 |
C | LYS109 |
C | PHE113 |
C | CYS143 |
C | TYR144 |
C | ASN174 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CAC D 1266 |
Chain | Residue |
D | GLU43 |
D | PHE49 |
D | LYS109 |
D | PHE113 |
D | CYS143 |
D | TYR144 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
A | LYS109 | |
A | GLU118 | |
A | GLU43 | |
A | CYS143 | |
A | ASN174 | |
A | ASN93 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
B | LYS109 | |
B | GLU118 | |
B | GLU43 | |
B | CYS143 | |
B | ASN174 | |
B | ASN93 |
site_id | CSA3 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
C | LYS109 | |
C | GLU118 | |
C | GLU43 | |
C | CYS143 | |
C | ASN174 | |
C | ASN93 |
site_id | CSA4 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
D | LYS109 | |
D | GLU118 | |
D | GLU43 | |
D | CYS143 | |
D | ASN174 | |
D | ASN93 |
site_id | CSA5 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
A | LYS109 | |
A | GLU118 | |
A | GLU43 | |
A | CYS143 | |
A | ASP167 | |
A | ASN93 |
site_id | CSA6 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
B | LYS109 | |
B | GLU118 | |
B | GLU43 | |
B | CYS143 | |
B | ASP167 | |
B | ASN93 |
site_id | CSA7 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
C | LYS109 | |
C | GLU118 | |
C | GLU43 | |
C | CYS143 | |
C | ASP167 | |
C | ASN93 |
site_id | CSA8 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
D | LYS109 | |
D | GLU118 | |
D | GLU43 | |
D | CYS143 | |
D | ASP167 | |
D | ASN93 |