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7CQB

Crystal structure of mutant of a Petase mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008126molecular_functionacetylesterase activity
A0016787molecular_functionhydrolase activity
A0042178biological_processxenobiotic catabolic process
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"29235460","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29374183","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29603535","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29666242","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"29235460","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29374183","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29603535","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29666242","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29235460","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29235460","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29666242","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2025-07-09

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