Structure of PDB 6l47 Chain B

Receptor sequence
>6l47B (length=416) Species: 9606 (Homo sapiens) [Search protein sequence]
QGKIFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRL
VLEFSLLSYAFGKFPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPL
IRSLFHGFLFMIFQIGVLGFGPTYVVLAYTLPPASRFIIIFEQIRFVMKA
HSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYFLFAPTLIYRDSYPRNPT
VRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVF
NSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYY
RTWNVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVC
LSFFYPVLFVLFMFFGMAFNFPIWNVLMWTSLFLGNGVLLCFYSQEWYAR
QHCPLKDYVRPRSWTC
3D structure
PDB6l47 Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor.
ChainB
Resolution3.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.26: sterol O-acyltransferase.
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 CLR B H137 T140 I141 H20 T23 I24
BS02 E5L B T380 Y417 W420 N421 V424 H460 N511 T263 Y300 W303 N304 V307 H343 N386 BindingDB: IC50=200nM
BS03 CLR B Y142 F145 C333 Y336 F378 F382 W408 Y25 F28 C216 Y219 F261 F265 W291
Gene Ontology
Molecular Function
GO:0008374 O-acyltransferase activity
GO:0034736 cholesterol O-acyltransferase activity
Biological Process
GO:0042632 cholesterol homeostasis
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6l47, PDBe:6l47, PDBj:6l47
PDBsum6l47
PubMed32424158
UniProtP35610|SOAT1_HUMAN Sterol O-acyltransferase 1 (Gene Name=SOAT1)

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