2GOK
Crystal structure of the imidazolonepropionase from Agrobacterium tumefaciens at 1.87 A resolution
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 | HOH610 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE B 501 |
Chain | Residue |
B | HOH581 |
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 |
B | ASP393 |
B | HOH522 |
B | HOH541 |
B | HOH544 |
B | HOH685 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 503 |
Chain | Residue |
A | ASN273 |
A | ASN273 |
A | HOH571 |
A | HOH571 |
A | HOH626 |
A | HOH626 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 504 |
Chain | Residue |
A | ARG200 |
A | ASP203 |
B | HOH685 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 505 |
Chain | Residue |
A | ASN94 |
A | PRO334 |
A | PRO338 |
A | THR340 |
B | TYR402 |
B | ARG403 |
B | HOH514 |
B | HOH516 |
B | HOH518 |
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 | HIS88 | |
A | HIS86 | |
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 |