2FTY
Crystal structure of dihydropyrimidinase from Saccharomyces kluyveri
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004157 | molecular_function | dihydropyrimidinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 |
| B | 0004157 | molecular_function | dihydropyrimidinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 |
| C | 0004157 | molecular_function | dihydropyrimidinase activity |
| C | 0005737 | cellular_component | cytoplasm |
| 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 |
| D | 0004157 | molecular_function | dihydropyrimidinase activity |
| D | 0005737 | cellular_component | cytoplasm |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | HIS62 |
| A | HIS64 |
| A | KCX167 |
| A | ASP358 |
| A | ZN602 |
| A | HOH1603 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 602 |
| Chain | Residue |
| A | ZN601 |
| A | HOH1603 |
| A | KCX167 |
| A | HIS199 |
| A | HIS255 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 601 |
| Chain | Residue |
| B | HIS62 |
| B | HIS64 |
| B | KCX167 |
| B | ASP358 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 602 |
| Chain | Residue |
| B | KCX167 |
| B | HIS199 |
| B | HIS255 |
| B | HOH2603 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 601 |
| Chain | Residue |
| C | HIS62 |
| C | HIS64 |
| C | KCX167 |
| C | ASP358 |
| C | HOH3603 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 602 |
| Chain | Residue |
| C | KCX167 |
| C | HIS199 |
| C | HIS255 |
| C | HOH3603 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 601 |
| Chain | Residue |
| D | HIS62 |
| D | HIS64 |
| D | KCX167 |
| D | ASP358 |
| D | HOH4603 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 602 |
| Chain | Residue |
| D | KCX167 |
| D | HIS199 |
| D | HIS255 |
| D | HOH4603 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16517602, ECO:0007744|PDB:2FTY, ECO:0007744|PDB:2FVK, ECO:0007744|PDB:2FVM |
| Chain | Residue | Details |
| A | HIS62 | |
| B | ASP358 | |
| C | HIS62 | |
| C | HIS64 | |
| C | HIS199 | |
| C | HIS255 | |
| C | ASP358 | |
| D | HIS62 | |
| D | HIS64 | |
| D | HIS199 | |
| D | HIS255 | |
| A | HIS64 | |
| D | ASP358 | |
| A | HIS199 | |
| A | HIS255 | |
| A | ASP358 | |
| B | HIS62 | |
| B | HIS64 | |
| B | HIS199 | |
| B | HIS255 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: via carbamate group => ECO:0000269|PubMed:16517602, ECO:0007744|PDB:2FTY, ECO:0007744|PDB:2FVK, ECO:0007744|PDB:2FVM |
| Chain | Residue | Details |
| A | KCX167 | |
| B | KCX167 | |
| C | KCX167 | |
| D | KCX167 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16517602, ECO:0007744|PDB:2FVK |
| Chain | Residue | Details |
| A | TYR172 | |
| D | TYR172 | |
| D | SER331 | |
| D | ASN392 | |
| A | SER331 | |
| A | ASN392 | |
| B | TYR172 | |
| B | SER331 | |
| B | ASN392 | |
| C | TYR172 | |
| C | SER331 | |
| C | ASN392 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:16517602, ECO:0007744|PDB:2FTY, ECO:0007744|PDB:2FVK, ECO:0007744|PDB:2FVM |
| Chain | Residue | Details |
| A | KCX167 | |
| B | KCX167 | |
| C | KCX167 | |
| D | KCX167 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| A | ASP358 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| B | ASP358 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| C | ASP358 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| D | ASP358 |
