Structure of PDB 4ls7 Chain A

Receptor sequence
>4ls7A (length=413) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
MTKKRVVVTGLGALSPLGNDVDTSWNNAINGVSGIGPITRVDAEEYPAKV
AAELKDFNVEDYMDKKEARKMDRFTQYAVVAAKMAVEDADLNITDEIAPR
VGVWVGSGIGGLETLESQFEIFLTKGPRRVSPFFVPMMIPDMATGQISIA
LGAKGVNSCTVTACATGTNSIGDAFKVIQRGDADVMVTGGTEAPLTRMSF
AGFSANKALSTNPDPKTASRPFDKNRDGFVMGEGAGIIVLEELEHALARG
AKIYGEIVGYGSTGDAYHITAPAQDGEGGARAMQEAIKDAGIAPEEIDYI
NAHGTSTYYNDKYETMAIKTVFGEHAHKLAVSSTKSMTGHLLGAAGGIEA
IFSILAIKEGVIPPTINIQTPDEECDLDYVPDEARRQELNYVLSNSLGFG
GHNATLIFKKYQS
3D structure
PDB4ls7 Structural insights into bacterial resistance to cerulenin.
ChainA
Resolution1.674 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 H302 E313 K334 H339 L396 F398
Catalytic site (residue number reindexed from 1) C164 H303 E314 K335 H340 L397 F399
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 1X9 A G107 I108 A162 C163 F202 H302 H339 L341 F398 G108 I109 A163 C164 F203 H303 H340 L342 F399
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:4ls7, PDBe:4ls7, PDBj:4ls7
PDBsum4ls7
PubMed24641521
UniProtO34340|FABF_BACSU 3-oxoacyl-[acyl-carrier-protein] synthase 2 (Gene Name=fabF)

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