2PUZ
Crystal structure of Imidazolonepropionase from Agrobacterium tumefaciens with bound product N-formimino-L-Glutamate
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 | histidine metabolic process |
| A | 0006548 | biological_process | 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 | histidine catabolic process to glutamate and formamide |
| A | 0019557 | biological_process | 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 | histidine metabolic process |
| B | 0006548 | biological_process | 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 | histidine catabolic process to glutamate and formamide |
| B | 0019557 | biological_process | 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 FE A 500 |
| Chain | Residue |
| A | HIS86 |
| A | HIS88 |
| A | HIS256 |
| A | ASP331 |
| A | HOH640 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 501 |
| Chain | Residue |
| B | NIG600 |
| B | HOH1183 |
| B | HIS86 |
| B | HIS88 |
| B | HIS256 |
| B | ASP331 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| A | ASP203 |
| A | HOH725 |
| A | HOH732 |
| B | ASP393 |
| B | HOH655 |
| B | HOH745 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 504 |
| Chain | Residue |
| A | ARG200 |
| A | ALA202 |
| A | ASP203 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NIG B 600 |
| Chain | Residue |
| B | HIS88 |
| B | ARG95 |
| B | TYR158 |
| B | HIS191 |
| B | PHE228 |
| B | ILE232 |
| B | ASN333 |
| B | GLY335 |
| B | THR336 |
| B | FE501 |
| B | HOH790 |
| B | HOH804 |
| B | HOH1183 |
| B | HOH1184 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00372 |
| Chain | Residue | Details |
| A | HIS86 | |
| A | HIS88 | |
| B | HIS86 | |
| B | HIS88 | |
| B | ARG95 | |
| B | HIS191 | |
| B | HIS256 | |
| B | GLN259 | |
| B | ASP331 | |
| B | THR336 | |
| A | ARG95 | |
| A | HIS191 | |
| A | HIS256 | |
| A | GLN259 | |
| A | ASP331 | |
| A | THR336 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18442260, ECO:0007744|PDB:2PUZ |
| Chain | Residue | Details |
| A | TYR158 | |
| A | ASN333 | |
| A | GLY335 | |
| B | TYR158 | |
| B | ASN333 | |
| B | GLY335 |
