1GKR
L-Hydantoinase (Dihydropyrimidinase) from Arthrobacter aurescens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000256 | biological_process | allantoin catabolic process |
| A | 0004038 | molecular_function | allantoinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006145 | biological_process | purine nucleobase 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 | 0050897 | molecular_function | cobalt ion binding |
| B | 0000256 | biological_process | allantoin catabolic process |
| B | 0004038 | molecular_function | allantoinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006145 | biological_process | purine nucleobase 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 | 0050897 | molecular_function | cobalt ion binding |
| C | 0000256 | biological_process | allantoin catabolic process |
| C | 0004038 | molecular_function | allantoinase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006145 | biological_process | purine nucleobase catabolic process |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0050897 | molecular_function | cobalt ion binding |
| D | 0000256 | biological_process | allantoin catabolic process |
| D | 0004038 | molecular_function | allantoinase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006145 | biological_process | purine nucleobase catabolic process |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1452 |
| Chain | Residue |
| A | KCX147 |
| A | HIS183 |
| A | HIS239 |
| A | ZN1453 |
| A | HOH2124 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1453 |
| Chain | Residue |
| A | ZN1452 |
| A | HOH2124 |
| A | HIS60 |
| A | HIS62 |
| A | KCX147 |
| A | ASP312 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1452 |
| Chain | Residue |
| B | KCX147 |
| B | HIS183 |
| B | HIS239 |
| B | ZN1453 |
| B | HOH2129 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 1453 |
| Chain | Residue |
| B | HIS60 |
| B | HIS62 |
| B | KCX147 |
| B | ASP312 |
| B | ZN1452 |
| B | HOH2129 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 1452 |
| Chain | Residue |
| C | KCX147 |
| C | HIS183 |
| C | HIS239 |
| C | ZN1453 |
| C | HOH2128 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 1453 |
| Chain | Residue |
| C | HIS60 |
| C | HIS62 |
| C | KCX147 |
| C | ASP312 |
| C | ZN1452 |
| C | HOH2128 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 1452 |
| Chain | Residue |
| D | KCX147 |
| D | HIS183 |
| D | HIS239 |
| D | ZN1453 |
| D | HOH2127 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN D 1453 |
| Chain | Residue |
| D | HIS60 |
| D | HIS62 |
| D | KCX147 |
| D | ASP312 |
| D | ZN1452 |
| D | HOH2127 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12093275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GKR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"12093275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GKR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"12093275","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GKR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| A | ASP312 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| B | ASP312 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| C | ASP312 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| D | ASP312 |
