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4K6H

Crystal structure of CALB mutant L278M from Candida antarctica

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriacylglycerol lipase activity
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
B0004806molecular_functiontriacylglycerol lipase activity
B0006629biological_processlipid metabolic process
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
AILE314

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
AGLY39
ATHR40
ATRP104
ASER105
AMET278
AALA281

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
BARG127
BTHR244
ALYS13
BASP126

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 401
ChainResidue
BSER67
BPRO69
BPRO70
BPHE71

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 402
ChainResidue
BASN169
BPRO303
BPHE304
BALA305
BVAL306

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
BTHR40
BTRP104
BSER105

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 404
ChainResidue
BPRO198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PubMed","id":"8527460","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8087556","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8527460","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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