2OCG
Crystal structure of human valacyclovir hydrolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005741 | cellular_component | mitochondrial outer membrane |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017171 | molecular_function | serine hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047658 | molecular_function | alpha-amino-acid esterase activity |
| A | 0050667 | biological_process | homocysteine metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | HIS35 |
| A | GLU57 |
| A | ASP78 |
| A | HIS84 |
| A | HOH588 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | ASP204 |
| A | HOH635 |
| A | HOH636 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 501 |
| Chain | Residue |
| A | ASP123 |
| A | ILE126 |
| A | GLY146 |
| A | ALA147 |
| A | ASN148 |
| A | TRP192 |
| A | VAL230 |
| A | HIS255 |
| A | HOH607 |
| A | HOH750 |
| A | SER122 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. VSLLGWSDGG |
| Chain | Residue | Details |
| A | VAL116-GLY125 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 119 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18256025","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10037","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18256025","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2OCG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OCI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OCK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OCL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Binding of alpha-amino group of substrate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8R164","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8R164","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8R164","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| A | SER122 | |
| A | HIS255 | |
| A | ASP227 |
