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1K8Q

CRYSTAL STRUCTURE OF DOG GASTRIC LIPASE IN COMPLEX WITH A PHOSPHONATE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0005576cellular_componentextracellular region
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0043231cellular_componentintracellular membrane-bounded organelle
B0004806molecular_functiontriglyceride lipase activity
B0005576cellular_componentextracellular region
B0016042biological_processlipid catabolic process
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0043231cellular_componentintracellular membrane-bounded organelle
Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. LHYVGHSQGT
ChainResidueDetails
ALEU147-THR156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:11689574
ChainResidueDetails
ASER153
BSER153

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:11689574
ChainResidueDetails
AASP324
AHIS353
BASP324
BHIS353

site_idSWS_FT_FI3
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN15
AASN80
AASN252
AASN308
BASN15
BASN80
BASN252
BASN308

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
AHIS353
AASP333
ASER153

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
BHIS353
BASP333
BSER153

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
AHIS353
AGLN154
AASP333
ALEU67
ASER153

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1tah
ChainResidueDetails
BHIS353
BGLN154
BASP333
BLEU67
BSER153

222415

PDB entries from 2024-07-10

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