Structure of PDB 6h18 Chain A

Receptor sequence
>6h18A (length=523) Species: 9606 (Homo sapiens) [Search protein sequence]
QSKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTKALENPQPHP
GWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLP
VMIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLG
FLSTGDANLPGNYGLRDQHMAIAWVKRNIAAFGGDPDNITLFGESAGGAS
VSLQTLSPYNKGLIRRAISQSGVALSPWVIQKNPLFWAKKVAEKVGCPVG
DAARMAQCLKVTDPRALTLAYKVPLAGLEYPMLHYVGFVPVIDGDFIPDD
PINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVTEEDFYKLVS
EFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEI
ALAQHRANAKSAKTYAYLFSHPADHADDIQYVFGKPFATPTGYRPQDRTV
SKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSM
KRSLRTNFLRYWTLTYLALPTVT
3D structure
PDB6h18 X-ray structures of human bile-salt activated lipase conjugated to nerve agents surrogates.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G107 A108 S194 A195 D320 H435
Catalytic site (residue number reindexed from 1) G108 A109 S195 A196 D321 H425
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 ZN A D77 E78 D78 E79
BS02 ZN A H420 H435 R454 D457 H421 H425 R444 D447
BS03 ZN A H487 E489 H477 E479
BS04 ZN A E193 D437 D438 E194 D427 D428
External links
PDB RCSB:6h18, PDBe:6h18, PDBj:6h18
PDBsum6h18
PubMed30359675
UniProtP19835|CEL_HUMAN Bile salt-activated lipase (Gene Name=CEL)

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