Structure of PDB 4piv Chain A

Receptor sequence
>4pivA (length=610) Species: 9606 (Homo sapiens) [Search protein sequence]
MQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTPSQQELPR
LLSAACRLAQVLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKM
KVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQH
DVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGG
FLLLHTLLRGHPLGDIVAFLTSQGILSQDAWESLFSRVSLRLVGLKKSFY
GSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSARPVWLKAI
NCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKV
LQGDLVMNVYRDGAWGAFRHFLLEEDSKTFCPAHKSYIIAGGLGGFGLEL
AQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLE
GARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTL
NLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRH
EGLPGLAVQWGAIGDVGILVETNDTIVSGTLPQRMASCLEVLDLFLNQPH
MVLSSFVLAE
3D structure
PDB4piv A human fatty acid synthase inhibitor binds beta-ketoacyl reductase in the keto-substrate site.
ChainA
Resolution2.299 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K1995 S2021 Y2034 N2038
Catalytic site (residue number reindexed from 1) K495 S521 Y534 N538
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
External links
PDB RCSB:4piv, PDBe:4piv, PDBj:4piv
PDBsum4piv
PubMed25086508
UniProtP49327|FAS_HUMAN Fatty acid synthase (Gene Name=FASN)

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