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3QPD

Structure of Aspergillus oryzae cutinase expressed in Pichia pastoris, crystallized in the presence of Paraoxon

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016042biological_processlipid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00155
Number of Residues13
DetailsCUTINASE_1 Cutinase, serine active site. PdTqIVaGGYSQG
ChainResidueDetails
APRO116-GLY128

site_idPS00931
Number of Residues18
DetailsCUTINASE_2 Cutinase, aspartate and histidine active sites. CavgDlVClGTliVappH
ChainResidueDetails
ACYS177-HIS194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"19810726","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GBS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"19810726","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GBS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"19810726","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GBS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00590","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-07-23

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