Structure of PDB 1ox0 Chain A

Receptor sequence

>1ox0A (length=414) Species: 1313 (Streptococcus pneumoniae)

PRGSHMKLNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSD
FDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQEAVNHANLDVEA
LNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASG
NVAMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASI
TPFAIAGFQALTALSTTEDPTRASIPFDKDRNGFVMGEGSGMLVLESLEH
AEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPE
QVAYVNAHGTSTPANEKGESGAIVAVLGKEVPVSSTKSFTGHLLGAAGAV
EAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFG
FGGHNAVLAFKRWE

3D structure

• PDB: 1ox0 The 1.3-Angstrom-Resolution Crystal Structure of beta-Ketoacyl-Acyl Carrier Protein Synthase II from Streptococcus pneumoniae.
• Chain: A
• Resolution: 1.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C164 H303 E314 K332 H337 F394 F396
• Catalytic site (residue number reindexed from 1): C169 H308 E319 K337 H342 F399 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	MG	A	N301 A302 E346 N392	N306 A307 E351 N397

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
• GO:0046872 metal ion binding

Biological Process

• GO:0006633 fatty acid biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1ox0, PDBe:1ox0, PDBj:1ox0
• PDBsum: 1ox0
• PubMed: 12837788
• UniProt: Q9FBC2