Structure of PDB 3il5 Chain D

Receptor sequence
>3il5D (length=320) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
KNYARISCTSRYVPENCVTNHQLSEMMDTSDEWIHSRTGISERRIVTQEN
TSDLCHQVAKQLLEKSGKQASEIDFILVATVTPDFNMPSVACQVQGAIGA
TEAFAFDISAACSGFVYALSMAEKLVLSGRYQTGLVIGGETFSKMLDWTD
RSTAVLFGDGAAGVLIEAAETPHFLNEKLQADGQRWAALTSGYTINESPF
YQGHKQASKTLQMEGRSIFDFAIKDVSQNILSLVTDETVDYLLLHQANVR
IIDKIARKTKISREKFLTNMDKYGNTSAASIPILLDEAVENGTLILGSQQ
RVVLTGFGGGLTWGSLLLTL
3D structure
PDB3il5 Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
ChainD
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.180: beta-ketoacyl-[acyl-carrier-protein] synthase III.
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 B82 D R42 L161 G220 I223 F224 A252 R255 I256 N280 F312 G313 R37 L156 G215 I218 F219 A247 R250 I251 N275 F307 G308 BindingDB: IC50=1600nM
Gene Ontology
Molecular Function
GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
GO:0016746 acyltransferase activity
GO:0033818 beta-ketoacyl-acyl-carrier-protein synthase III activity
Biological Process
GO:0006633 fatty acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:3il5, PDBe:3il5, PDBj:3il5
PDBsum3il5
PubMed19665020
UniProtQ820T1|FABH_ENTFA Beta-ketoacyl-[acyl-carrier-protein] synthase III (Gene Name=fabH)

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