Structure of PDB 2jfk Chain D

Receptor sequence
>2jfkD (length=410) Species: 9606 (Homo sapiens) [Search protein sequence]
LGTENLYFQSMRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAV
PATAMPFRGYAVLGGERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSL
MRLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQ
IGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCI
KEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSA
RWLSTSIPEAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLE
IAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGIGRLHLSGIDA
NPNALFPPVE
3D structure
PDB2jfk Structure of the MAT Domain of Human Fas with Malonyl-Coa
ChainD
Resolution2.4 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 COA D V675 R676 V265 R266
Gene Ontology
Molecular Function
GO:0016740 transferase activity

View graph for
Molecular Function
External links
PDB RCSB:2jfk, PDBe:2jfk, PDBj:2jfk
PDBsum2jfk
PubMed
UniProtP49327|FAS_HUMAN Fatty acid synthase (Gene Name=FASN)

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