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3MIL

Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0005575cellular_componentcellular_component
A0006083biological_processacetate metabolic process
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
B0005575cellular_componentcellular_component
B0006083biological_processacetate metabolic process
B0006629biological_processlipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 241
ChainResidue
ASER12
ALYS52
AGLY53
AASN83
AGLN91
AARG143
AHIS190
AHOH637

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 241
ChainResidue
BLYS52
BGLY53
BASN83
BGLN91
BTRP129
BARG143
BHIS190
BHOH430
BSER12

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21069734","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21069734","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21069734","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"21069734","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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