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 | L-tryptophan catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019441 | biological_process | L-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 | L-tryptophan catabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019441 | biological_process | L-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 | L-tryptophan catabolic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019441 | biological_process | L-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 | L-tryptophan catabolic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019441 | biological_process | L-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 | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01969","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24942958","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24942958","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CZ1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01969","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24942958","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CZ1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
