Structure of PDB 1aql Chain A

Receptor sequence
>1aqlA (length=532) Species: 9913 (Bos taurus) [Search protein sequence]
AKLGSVYTEGGFVEGVNKKLSLFGDSIDIFKGIPFAAAPKALEKPERHPG
WQGTLKAKSFKKRCLQATLTQDSTYGNEDCLYLNIWVPQGRKEVSHDLPV
MIWIYGGAFLMGASQGANFLSNYLYDGEEIATRGNVIVVTFNYRVGPLGF
LSTGDSNLPGNYGLWDQHMAIAWVKRNIEAFGGDPDNITLFGESAGGASV
SLQTLSPYNKGLIKRAISQSGVGLCPWAIQQDPLFWAKRIAEKVGCPVDD
TSKMAGCLKITDPRALTLAYKLPLGSTEYPKLHYLSFVPVIDGDFIPDDP
VNLYANAADVDYIAGTNDMDGHLFVGMDVPAINSNKQDVTEEDFYKLVSG
LTVTKGLRGANATYEVYTEPWAQDSSQETRKKTMVDLETDILFLIPTKIA
VAQHKSHAKSANTYTYLFSQPSRMPIYPKWMGADHADDLQYVFGKPFATP
LGYRAQDRTVSKAMIAYWTNFARTGDPNTGHSTVPANWDPYTLEDDNYLE
INKQMDSNSMKLHLRTNYLQFWTQTYQALPTV
3D structure
PDB1aql The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) G107 A108 G146 S194 A195 L285 F287 D320 H435
Catalytic site (residue number reindexed from 1) G107 A108 G146 S194 A195 L285 F287 D320 H435
Enzyme Commision number 3.1.1.13: sterol esterase.
3.1.1.3: triacylglycerol lipase.
3.1.1.6: acetylesterase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 TCH A F119 N122 L124 T449 F119 N122 L124 T449
BS02 TCH A D299 L351 T352 V353 T354 I391 P396 I399 D299 L351 T352 V353 T354 I391 P396 I399
Gene Ontology
Molecular Function
GO:0004771 sterol ester esterase activity
GO:0004806 triacylglycerol lipase activity
GO:0008126 acetylesterase activity
GO:0050253 retinyl-palmitate esterase activity
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0016042 lipid catabolic process
GO:0030157 pancreatic juice secretion
GO:0042572 retinol metabolic process
GO:0046514 ceramide catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1aql, PDBe:1aql, PDBj:1aql
PDBsum1aql
PubMed9331420
UniProtP30122|CEL_BOVIN Bile salt-activated lipase (Fragment) (Gene Name=CEL)

[Back to BioLiP]