Structure of PDB 4ls7 Chain B

Receptor sequence

>4ls7B (length=414) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168)

IQMTKKRVVVTGLGALSPLGNDVDTSWNNAINGVSGIGPITRVDAEEYPA
KVAAELKDFNVEDYMDKKEARKMDRFTQYAVVAAKMAVEDADLNITDEIA
PRVGVWVGSGIGGLETLESQFEIFLTKGPRRVSPFFVPMMIPDMATGQIS
IALGAKGVNSCTVTACATGTNSIGDAFKVIQRGDADVMVTGGTEAPLTRM
SFAGFSANKALSTNPDPKTASRPFDKNRDGFVMGEGAGIIVLEELEHALA
RGAKIYGEIVGYGSTGDAYHITAPAQDGEGGARAMQEAIKDAGIAPEEID
YINAHGTSTYYNDKYETMAIKTVFGEHAHKLAVSSTKSMTGHLLGAAGGI
EAIFSILAIKEGVIPPTINIQTPDEECDLDYVPDEARRQELNYVLSNSLG
FGGHNATLIFKKYQ

3D structure

• PDB: 4ls7 Structural insights into bacterial resistance to cerulenin.
• Chain: B
• Resolution: 1.674 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C163 H302 E313 K334 H339 L396 F398
• Catalytic site (residue number reindexed from 1): C166 H305 E316 K337 H342 L399 F401
• 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	B	I108 A162 C163 F202 H339 F398	I111 A165 C166 F205 H342 F401

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

External links

• PDB: RCSB:4ls7, PDBe:4ls7, PDBj:4ls7
• PDBsum: 4ls7
• PubMed: 24641521
• UniProt: O34340|FABF_BACSU 3-oxoacyl-[acyl-carrier-protein] synthase 2 (Gene Name=fabF)