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6ISR

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

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 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
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

250835

PDB entries from 2026-03-18

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