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2VEO

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0005576cellular_componentextracellular region
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
B0004806molecular_functiontriglyceride lipase activity
B0005576cellular_componentextracellular region
B0016042biological_processlipid catabolic process
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
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:17631665, ECO:0000305|PubMed:18155238
ChainResidueDetails
ATHR118
AARG268
APRO300
BTHR118
BARG268
BPRO300

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PDB entries from 2024-05-01

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