4CZ1
Crystal structure of kynurenine formamidase from Bacillus anthracis complexed with 2-aminoacetophenone.
Replaces: 4COAFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004061 | molecular_function | arylformamidase activity |
A | 0004328 | molecular_function | formamidase activity |
A | 0006569 | biological_process | tryptophan catabolic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
A | 0043420 | biological_process | anthranilate metabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004061 | molecular_function | arylformamidase activity |
B | 0004328 | molecular_function | formamidase activity |
B | 0006569 | biological_process | tryptophan catabolic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
B | 0043420 | biological_process | anthranilate metabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0004061 | molecular_function | arylformamidase activity |
C | 0004328 | molecular_function | formamidase activity |
C | 0006569 | biological_process | tryptophan catabolic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
C | 0043420 | biological_process | anthranilate metabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0004061 | molecular_function | arylformamidase activity |
D | 0004328 | molecular_function | formamidase activity |
D | 0006569 | biological_process | tryptophan catabolic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
D | 0043420 | biological_process | anthranilate metabolic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | ASP56 |
A | HIS161 |
A | GLU173 |
A | ZN402 |
A | HOH2046 |
A | HOH2103 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | GLU173 |
A | ZN401 |
A | HOH2027 |
A | HOH2046 |
A | HIS50 |
A | HIS54 |
A | ASP56 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE VNJ A 501 |
Chain | Residue |
A | TRP20 |
A | ASP23 |
A | HIS50 |
A | HIS60 |
A | HOH2046 |
B | VAL40 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | ASP56 |
B | HIS161 |
B | GLU173 |
B | ZN402 |
B | HOH2022 |
B | HOH2053 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | HIS50 |
B | HIS54 |
B | ASP56 |
B | GLU173 |
B | ZN401 |
B | HOH2016 |
B | HOH2022 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN C 401 |
Chain | Residue |
C | ASP56 |
C | HIS161 |
C | GLU173 |
C | ZN402 |
C | HOH2055 |
C | HOH2092 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN C 402 |
Chain | Residue |
C | HIS50 |
C | HIS54 |
C | ASP56 |
C | GLU173 |
C | ZN401 |
C | HOH2024 |
C | HOH2055 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 401 |
Chain | Residue |
D | ASP56 |
D | HIS161 |
D | GLU173 |
D | ZN402 |
D | HOH2033 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN D 402 |
Chain | Residue |
D | HIS50 |
D | HIS54 |
D | ASP56 |
D | GLU173 |
D | ZN401 |
D | HOH2022 |
D | HOH2033 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 1210 |
Chain | Residue |
C | GLY38 |
C | HOH2049 |
C | HOH2050 |
C | HOH2051 |
C | HOH2052 |
C | HOH2115 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 1210 |
Chain | Residue |
A | ASP64 |
A | HOH2054 |
A | HOH2055 |
A | HOH2132 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG D 1210 |
Chain | Residue |
D | ILE209 |
D | HOH2090 |
D | HOH2091 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000305|PubMed:24942958 |
Chain | Residue | Details |
A | HIS60 | |
B | HIS60 | |
C | HIS60 | |
D | HIS60 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CZ1 |
Chain | Residue | Details |
A | TRP20 | |
B | TRP20 | |
C | TRP20 | |
D | TRP20 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01969, ECO:0000269|PubMed:24942958, ECO:0007744|PDB:4CO9, ECO:0007744|PDB:4CZ1 |
Chain | Residue | Details |
A | HIS50 | |
B | GLU173 | |
C | HIS50 | |
C | HIS54 | |
C | ASP56 | |
C | HIS161 | |
C | GLU173 | |
D | HIS50 | |
D | HIS54 | |
D | ASP56 | |
D | HIS161 | |
A | HIS54 | |
D | GLU173 | |
A | ASP56 | |
A | HIS161 | |
A | GLU173 | |
B | HIS50 | |
B | HIS54 | |
B | ASP56 | |
B | HIS161 |