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3QPC

Structure of Fusarium Solani Cutinase expressed in Pichia pastoris, crystallized in the presence of Paraoxon

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00931
Number of Residues18
DetailsCUTINASE_2 Cutinase, aspartate and histidine active sites. CntgDlVCtGSliVaapH
ChainResidueDetails
ACYS171-HIS188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8286366","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OXM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CUT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8286366","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OXM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CUT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N-D-glucuronoyl glycine","evidences":[{"source":"PubMed","id":"7398618","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 631
ChainResidueDetails
ASER42electrostatic stabiliser
AMIR120covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
ALEU125electrostatic stabiliser
ATHR179electrostatic stabiliser, increase basicity
AGLY192proton acceptor, proton donor

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PDB entries from 2025-12-24

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