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4K6H

Crystal structure of CALB mutant L278M from Candida antarctica

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
B0004806molecular_functiontriglyceride lipase activity
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
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:8527460
ChainResidueDetails
ASER105
AASP187
BSER105
BASP187

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AHIS224
BHIS224

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8087556, ECO:0000269|PubMed:8527460
ChainResidueDetails
AASN74
BASN74

223166

PDB entries from 2024-07-31

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