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6ISQ

structure of Lipase mutant with oxided 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 Residues5
Detailsbinding site for residue ACT A 401
ChainResidue
ATHR40
ACSD105
AGLN157
AILE189
AIPA402

site_idAC2
Number of Residues6
Detailsbinding site for residue IPA A 402
ChainResidue
APRO280
AACT401
AGLY39
ATHR40
ACSD105
AHIS224

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 403
ChainResidue
ALYS136
AARG168
AHOH504
AHOH511
AHOH621
BASP296

site_idAC4
Number of Residues8
Detailsbinding site for residue EDO A 404
ChainResidue
AMET-1
ATHR174
AGLN175
AASN206
AHOH560
BALA92
BGLY95
BASN96

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 405
ChainResidue
AASP252
ATHR256
AASP257

site_idAC6
Number of Residues2
Detailsbinding site for residue PGE A 407
ChainResidue
AGLU188
AASP223

site_idAC7
Number of Residues5
Detailsbinding site for residue ACT B 401
ChainResidue
BTHR40
BCSD105
BGLN157
BILE189
BIPA402

site_idAC8
Number of Residues8
Detailsbinding site for residue IPA B 402
ChainResidue
BGLY39
BTHR40
BVAL104
BCSD105
BHIS224
BPRO280
BACT401
BHOH561

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:8527460
ChainResidueDetails
ACSD105
AASP187
BCSD105
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

219869

PDB entries from 2024-05-15

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