Structure of PDB 4w9n Chain D

Receptor sequence
>4w9nD (length=310) Species: 9606 (Homo sapiens) [Search protein sequence]
HAFVSTLTRGDLSSIRWVCCPGAQLCTVYYASLNFRDIMLATGKLSPDAI
PGKWTSQDSLLGMEFSGRDASGKRVMGLVPAKGLATSVLLSPDFLWDVPS
NWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIA
LSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSSFEQHVLWHTGGKGV
DLVLNSLAEEKLQASVRCLATHGRFLEIGKLGMAIFLKNVTFHGVLLDAF
FNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQHIGK
VVVQVLAEEP
3D structure
PDB4w9n Crystal structure of the human Fatty Acid synthase enoyl-acyl carrier protein-reductase domain complexed with triclosan reveals allosteric protein-protein interface inhibition.
ChainD
Resolution1.84 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase.
1.3.1.39: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific).
2.3.1.38: [acyl-carrier-protein] S-acetyltransferase.
2.3.1.39: [acyl-carrier-protein] S-malonyltransferase.
2.3.1.41: beta-ketoacyl-[acyl-carrier-protein] synthase I.
2.3.1.85: fatty-acid synthase system.
3.1.2.14: oleoyl-[acyl-carrier-protein] hydrolase.
4.2.1.59: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase.
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 TCL D L1753 F1766 F1791 L212 F225 F242 MOAD: ic50=54.7uM
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:4w9n, PDBe:4w9n, PDBj:4w9n
PDBsum4w9n
PubMed25301948
UniProtP49327|FAS_HUMAN Fatty acid synthase (Gene Name=FASN)

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