Structure of PDB 1fj8 Chain A

Receptor sequence
>1fj8A (length=403) Species: 562 (Escherichia coli) [Search protein sequence]
KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGN
VKLDTTGLIDRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVGL
IAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPFK
IHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEF
DAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVEELEHALARGA
HIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGTS
TPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLMLE
HGFIAPSINIEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVM
RKL
3D structure
PDB1fj8 Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism.
ChainA
Resolution2.27 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C163 H298 E309 K328 H333 F390 F392
Catalytic site (residue number reindexed from 1) C162 H297 E308 K327 H332 F389 F391
Enzyme Commision number 2.3.1.41: beta-ketoacyl-[acyl-carrier-protein] synthase I.
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 CER A G106 G107 A162 C163 E200 F201 H298 H333 G391 F392 G105 G106 A161 C162 E199 F200 H297 H332 G390 F391
Gene Ontology
Molecular Function
GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0044281 small molecule metabolic process
GO:1903966 monounsaturated fatty acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fj8, PDBe:1fj8, PDBj:1fj8
PDBsum1fj8
PubMed11050088
UniProtP0A953|FABB_ECOLI 3-oxoacyl-[acyl-carrier-protein] synthase 1 (Gene Name=fabB)

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