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 | 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 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 | |
B | HIS88 | |
B | ARG95 | |
B | HIS191 | |
B | HIS256 | |
B | GLN259 | |
B | ASP331 | |
B | THR336 | |
A | HIS88 | |
A | ARG95 | |
A | HIS191 | |
A | HIS256 | |
A | GLN259 | |
A | ASP331 | |
A | THR336 | |
B | HIS86 |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
A | ASP331 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1j79 |
Chain | Residue | Details |
B | ASP331 |