Structure of PDB 2ix4 Chain A

Receptor sequence
>2ix4A (length=431) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTLDDLKMKSFDEETK
LYTFDQLSSKVAAFVPYGSNPGEFDEALWLNSKAVANFIGYAVCAADEAL
RDAEWLPTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFI
PKILVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADV
MVAGGTESSIDALSVAGFSRSRALSTKFNSSPQEASRPFDCDRDGFVIGE
GSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAM
TRALRQSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEHATSGTLAF
SSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKRFMP
LTTSKKMLVRTAMSNSFGFGGTNASLLFASI
3D structure
PDB2ix4 Structure of the Human Beta-Ketoacyl [Acp] Synthase from the Mitochondrial Type II Fatty Acid Synthase.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C209 H350 E361 K384 H389 F447 F449
Catalytic site (residue number reindexed from 1) C179 H320 E331 K354 H359 F417 F419
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 6NA A I154 A208 C209 F248 G448 F449 I124 A178 C179 F218 G418 F419
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:0010027 thylakoid membrane organization
Cellular Component
GO:0005739 mitochondrion

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Molecular Function
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Cellular Component
External links
PDB RCSB:2ix4, PDBe:2ix4, PDBj:2ix4
PDBsum2ix4
PubMed17242430
UniProtQ8L3X9|KASM_ARATH 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial (Gene Name=KAS)

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