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 | 0046872 | molecular_function | metal ion binding |
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 | 0046872 | molecular_function | metal ion binding |
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 | 0046872 | molecular_function | metal ion binding |
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 | 0046872 | molecular_function | metal ion binding |
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: BINDING => ECO:0000269|PubMed:12093275, ECO:0007744|PDB:1GKR |
Chain | Residue | Details |
A | HIS60 | |
B | ASP312 | |
C | HIS60 | |
C | HIS62 | |
C | HIS183 | |
C | HIS239 | |
C | ASP312 | |
D | HIS60 | |
D | HIS62 | |
D | HIS183 | |
D | HIS239 | |
A | HIS62 | |
D | ASP312 | |
A | HIS183 | |
A | HIS239 | |
A | ASP312 | |
B | HIS60 | |
B | HIS62 | |
B | HIS183 | |
B | HIS239 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:12093275, ECO:0007744|PDB:1GKR |
Chain | Residue | Details |
A | KCX147 | |
B | KCX147 | |
C | KCX147 | |
D | KCX147 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12093275, ECO:0007744|PDB:1GKR |
Chain | Residue | Details |
A | KCX147 | |
B | KCX147 | |
C | KCX147 | |
D | KCX147 |
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 |