› 3uwd

X-ray diffraction
1.68Å resolution

Crystal Structure of Phosphoglycerate Kinase from Bacillus Anthracis

Released:
DOI: 10.2210/pdb3uwd/pdb
PDB entry 3uwd coloured by chain, front view.
PDB entry 3uwd coloured by chain, side view.
PDB entry 3uwd coloured by chain, top view.
Source organism: Bacillus anthracis
Primary publication:
Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni.
Zheng H, Filippova EV, Tkaczuk KL, Dworzynski P, Chruszcz M, Porebski PJ, Wawrzak Z, Onopriyenko O, Kudritska M, Grimshaw S, Savchenko A, Anderson WF, Minor W
J Struct Funct Genomics 13 15-26 (2012)
PMID: 22403005

Function and Biology Details

Reaction catalysed: 
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-182619 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate kinase Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 42.88 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q81X75 (Residues: 1-394; Coverage: 100%)
Gene names: BAS4988, BA_5367, GBAA_5367, pgk
Sequence domains: Phosphoglycerate kinase
Structure domains: Phosphoglycerate kinase, N-terminal domain

Ligands and Environments

4 bound ligands:
Ligand CL 5 x CL
Ligand MG 1 x MG
Ligand BTB 1 x BTB
Ligand UNL 1 x UNL
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 119.687Å b: 45.334Å c: 68.607Å
α: 90° β: 97.95° γ: 90°
R-values:
R R work R free
0.176 0.174 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Ancient Regulatory Role of Lysine Acetylation in Central Metabolism.
Nakayasu et al. (2017)
3 more

3 mentions without citation

Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.
Rojas-Pirela et al. (2020)
2 more