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2VEO

X-ray structure of Candida antarctica lipase A in its closed state.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriacylglycerol lipase activity
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
B0004806molecular_functiontriacylglycerol lipase activity
B0005576cellular_componentextracellular region
B0006629biological_processlipid metabolic process
B0016042biological_processlipid catabolic process
B0016298molecular_functionlipase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IUM A 1441
ChainResidue
AASP292
AGLU298

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IUM A 1442
ChainResidue
AASP220
AGLU314

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IUM B 1441
ChainResidue
BASP292
BGLU298

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IUM B 1442
ChainResidue
BASP220
BGLU314

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG4 A 1443
ChainResidue
APHE149
ASER184
AALA218
ATHR221
APHE222
APHE233
AGLY237
AVAL238
AASP95

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1443
ChainResidue
BASP95
BPHE149
BSER184
BGLY185
BTHR221
BPHE431

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"17631665","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18155238","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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