› 1oxh

X-ray diffraction
2.09Å resolution

The crystal structure of beta-ketoacyl-[acyl carrier protein] synthase II from Streptococcus Pneumoniae, Triclinic form

Released:
DOI: 10.2210/pdb1oxh/pdb
PDB entry 1oxh coloured by chain, front view.
PDB entry 1oxh coloured by chain, side view.
PDB entry 1oxh coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae.
Price AC, Rock CO, White SW
J Bacteriol 185 4136-43 (2003)
PMID: 12837788

Function and Biology Details

Reaction catalysed: 
A (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO(2) + an [acyl-carrier protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190278 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 430 amino acids
Theoretical weight: 46.02 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FBC2 (Residues: 1-411; Coverage: 100%)
Gene names: A5N45_03205, AZJ28_03470, AZJ70_07650, AZK02_07750, ERS019209_01512, ERS019261_01074, ERS019316_01650, ERS019486_01303, ERS019694_00480, ERS020302_00911, ERS020893_01786, ERS020941_00999, ERS021218_01784, ERS043904_02518, ERS096071_01417, GM536_04995, GM539_04300, GM540_01020, GM543_03230, GM544_00755, GM545_01935, RLD18_05995, SAMEA1462998_00705, SAMEA2627268_00398, SAMEA3171064_01875, SAMEA3353485_01245, SAMEA3354366_00476, SAMEA3381574_00886, SAMEA3389245_02216, SAMEA3390019_00019, fabF, fabF_3
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P1
Unit cell:
a: 61.52Å b: 71.646Å c: 96.1Å
α: 89.83° β: 83.09° γ: 69.15°
R-values:
R R work R free
0.209 0.208 0.235
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The structural biology of type II fatty acid biosynthesis.
White et al. (2005)
7 more

3 mentions without citation

Structural classification and properties of ketoacyl synthases.
Chen et al. (2011)
2 more