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6ISR

structure of lipase mutant with Cys-His-Asp catalytic triad

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 Residues3
Detailsbinding site for residue NI A 401
ChainResidue
ACYS105
AHIS224
AHOH525

site_idAC2
Number of Residues4
Detailsbinding site for residue PEG A 402
ChainResidue
AASP17
ALEU20
APRO27
ATHR89

site_idAC3
Number of Residues3
Detailsbinding site for residue PG4 A 403
ChainResidue
AALA170
ATHR116
AARG122

site_idAC4
Number of Residues3
Detailsbinding site for residue NI B 401
ChainResidue
BCYS105
BHIS224
BHOH525

site_idAC5
Number of Residues5
Detailsbinding site for residue PEG B 402
ChainResidue
BLYS32
BARG127
BARG242
BSER243
BTHR244

site_idAC6
Number of Residues2
Detailsbinding site for residue PEG B 403
ChainResidue
BVAL194
BGLN211

site_idAC7
Number of Residues2
Detailsbinding site for residue PG4 B 404
ChainResidue
BARG122
BALA170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:8527460
ChainResidueDetails
ACYS105
AASP187
BCYS105
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

222926

PDB entries from 2024-07-24

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