› 1j3n

X-ray diffraction
2Å resolution

Crystal Structure of 3-oxoacyl-(acyl-carrier protein) Synthase II from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1j3n/pdb
PDB entry 1j3n coloured by chain, front view.
PDB entry 1j3n coloured by chain, side view.
PDB entry 1j3n coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.
Bagautdinov B, Ukita Y, Miyano M, Kunishima N
Acta Crystallogr Sect F Struct Biol Cryst Commun 64 358-66 (2008)
PMID: 18453702

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

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-178137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 408 amino acids
Theoretical weight: 43.26 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SL80 (Residues: 1-408; Coverage: 100%)
Gene name: TTHA0413
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand CIT 1 x CIT
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P21212
Unit cell:
a: 72.067Å b: 185.573Å c: 62.517Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.258
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

PGLN: A newly identified amino phosphoglycolipid species in Thermus thermophilus HB8.
Nemoto et al. (2022)
1 more

8 mentions without citation

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