2G3F
Crystal Structure of imidazolonepropionase complexed with imidazole-4-acetic acid sodium salt, a substrate homologue
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006547 | biological_process | L-histidine metabolic process |
| A | 0006548 | biological_process | L-histidine catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| A | 0019556 | biological_process | L-histidine catabolic process to glutamate and formamide |
| A | 0019557 | biological_process | L-histidine catabolic process to glutamate and formate |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050480 | molecular_function | imidazolonepropionase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006547 | biological_process | L-histidine metabolic process |
| B | 0006548 | biological_process | L-histidine catabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| B | 0019556 | biological_process | L-histidine catabolic process to glutamate and formamide |
| B | 0019557 | biological_process | L-histidine catabolic process to glutamate and formate |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050480 | molecular_function | imidazolonepropionase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1601 |
| Chain | Residue |
| A | HIS80 |
| A | HIS82 |
| A | HIS249 |
| A | ASP324 |
| A | HOH1739 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 2601 |
| Chain | Residue |
| B | HOH2717 |
| B | HIS80 |
| B | HIS82 |
| B | HIS249 |
| B | ASP324 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IZC A 1500 |
| Chain | Residue |
| A | ARG89 |
| A | TYR102 |
| A | ILE112 |
| A | TYR152 |
| A | HIS185 |
| A | PHE221 |
| A | GLU252 |
| A | ASN326 |
| A | SER329 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE IZC B 2500 |
| Chain | Residue |
| B | ARG89 |
| B | TYR102 |
| B | ILE112 |
| B | TYR152 |
| B | HIS185 |
| B | PHE221 |
| B | GLU252 |
| B | ASN326 |
| B | SER329 |
| B | HOH2717 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16990261, ECO:0007744|PDB:2BB0, ECO:0007744|PDB:2G3F |
| Chain | Residue | Details |
| A | HIS80 | |
| A | HIS82 | |
| A | HIS249 | |
| A | ASP324 | |
| B | HIS80 | |
| B | HIS82 | |
| B | HIS249 | |
| B | ASP324 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:16990261, ECO:0007744|PDB:2G3F |
| Chain | Residue | Details |
| A | ARG89 | |
| A | HIS185 | |
| A | GLU252 | |
| B | ARG89 | |
| B | HIS185 | |
| B | GLU252 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00372 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | ASN326 | |
| A | GLY328 | |
| A | SER329 | |
| B | TYR152 | |
| B | ASN326 | |
| B | GLY328 | |
| B | SER329 |
