Structure of PDB 4ls8 Chain A

Receptor sequence
>4ls8A (length=416) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
GIQMTKKRVVVTGLGALSPLGNDVDTSWNNAINGVSGIGPITRVDAEEYP
AKVAAELKDFNVEDYMDKKEARKMDRFTQYAVVAAKMAVEDADLNITDEI
APRVGVWVGSGIGGLETLESQFEIFLTKGPRRVSPFFVPMMIPDMATGQI
SIALGAKGVNSCTVTACATGTNSIGDAFKVIQRGDADVMVTGGTEAPLTR
MSFAGFSANKALSTNPDPKTASRPFDKNRDGFVMGEGAGIIVLEELEHAL
ARGAKIYGEIVGYGSTGDAYHITAPAQDGEGGARAMQEAIKDAGIAPEEI
DYINAHGTSTYYNDKYETMAIKTVFGEHAHKLAVSSTKSMTGHLLGAAGG
IEAIFSILAIKEGVIPPTINIQTPDEECDLDYVPDEARRQELNYVLSNSL
GFGGHNATLIFKKYQS
3D structure
PDB4ls8 Structural insights into bacterial resistance to cerulenin.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C164 H303 E314 K335 H340 L397 F399
Catalytic site (residue number reindexed from 1) C167 H306 E317 K338 H343 L400 F402
Enzyme Commision number 2.3.1.179: beta-ketoacyl-[acyl-carrier-protein] synthase II.
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 1XG A I109 A163 C164 F203 H303 G398 F399 I112 A166 C167 F206 H306 G401 F402
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
Cellular Component
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:4ls8, PDBe:4ls8, PDBj:4ls8
PDBsum4ls8
PubMed24641521
UniProtO34340|FABF_BACSU 3-oxoacyl-[acyl-carrier-protein] synthase 2 (Gene Name=fabF)

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