› 5ikl

X-ray diffraction
2.4Å resolution

Crystal structure of P. aeruginosa geranyl-CoA carboxylase (GCC), beta subunit

Released:
DOI: 10.2210/pdb5ikl/pdb
PDB 5ikl coloured by chain and viewed from the front.
PDB 5ikl coloured by chain and viewed from the side.
PDB 5ikl coloured by chain and viewed from the top.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structure and substrate selectivity of the 750-kDa ��6��6 holoenzyme of geranyl-CoA carboxylase.
Jurado AR, Huang CS, Zhang X, Zhou ZH, Tong L
Nat Commun 6 8986 (2015)
PMID: 26593090

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Geranyl-CoA carboxylase, beta-subunit Chains: B, D, F
Molecule details ›
Chains: B, D, F
Length: 537 amino acids
Theoretical weight: 57.26 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HZV9 (Residues: 2-538; Coverage: 100%)
Gene names: PA2888, atuC
Sequence domains: Carboxyl transferase domain
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P6522
Unit cell:
a: 105.722Å b: 105.722Å c: 550.76Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.215 0.282
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation.
Wei et al. (2016)
2 more