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4K6K

Crystal structure of CALB mutant D223G 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 Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
AALA18
AEDO402
AEDO404
AHOH577
AHOH626
BEDO401

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
AEDO401
AEDO407
AEDO408

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
ATYR203
AGLY207
ALYS208
AASN209
AHOH578

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
ATYR203
APHE205
AEDO401
AHOH554
BTHR316
BEDO401

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 405
ChainResidue
ATYR91
AASN96
AEDO408
AHOH635

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 406
ChainResidue
AEDO408

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 407
ChainResidue
AALA18
AEDO402

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 408
ChainResidue
AEDO402
AEDO405
AEDO406

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 401
ChainResidue
AEDO401
AEDO404
AHOH589
BPRO317
BLEU318
BHOH561

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:8527460
ChainResidueDetails
BSER105
BASP187
ASER105
AASP187

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

219869

PDB entries from 2024-05-15

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