2VR2
Human Dihydropyrimidinase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004157 | molecular_function | dihydropyrimidinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006208 | biological_process | pyrimidine nucleobase catabolic process |
| A | 0006210 | biological_process | thymine catabolic process |
| A | 0006212 | biological_process | uracil catabolic process |
| A | 0006248 | biological_process | CMP catabolic process |
| A | 0006249 | biological_process | dCMP 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 | 0042802 | molecular_function | identical protein binding |
| A | 0046050 | biological_process | UMP catabolic process |
| A | 0046079 | biological_process | dUMP catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051219 | molecular_function | phosphoprotein binding |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1494 |
| Chain | Residue |
| A | HIS67 |
| A | HIS69 |
| A | LYS159 |
| A | ASP326 |
| A | ZN1495 |
| A | HOH2001 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1495 |
| Chain | Residue |
| A | ZN1494 |
| A | LYS159 |
| A | HIS192 |
| A | HIS248 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 1496 |
| Chain | Residue |
| A | LYS88 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human dihydropyrimidinase.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2VR2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human dihydropyrimidinase.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2VR2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9P903","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9EQF5","evidenceCode":"ECO:0000250"}]} |
| 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 | ASP326 |
