› 2bzb

Solution NMR

NMR Solution Structure of a protein aspartic acid phosphate phosphatase from Bacillus Anthracis

Released:
DOI: 10.2210/pdb2bzb/pdb
PDB entry 2bzb coloured by chain, ensemble of 32 models, front view.
PDB entry 2bzb coloured by chain, ensemble of 32 models, side view.
PDB entry 2bzb coloured by chain, ensemble of 32 models, top view.
Source organism: Bacillus anthracis str. Ames
Primary publication:
Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli.
Grenha R, Rzechorzek NJ, Brannigan JA, de Jong RN, Ab E, Diercks T, Truffault V, Ladds JC, Fogg MJ, Bongiorni C, Perego M, Kaptein R, Wilson KS, Folkers GE, Wilkinson AJ
J Biol Chem 281 37993-8003 (2006)
PMID: 17001075

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105242 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Conserved domain protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 62 amino acids
Theoretical weight: 7.52 KDa
Source organism: Bacillus anthracis str. Ames
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A4Y1VZT9 (Residues: 19-72; Coverage: 75%)
Gene name: GBAA_1655
Sequence domains: Spo0E like sporulation regulatory protein
Structure domains: Helix-loop-helix DNA-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: CANDID
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Molecular Mechanisms of Two-Component Signal Transduction.
Zschiedrich et al. (2016)
1 more

1 mention without citation

Simultaneous prediction of protein folding and docking at high resolution.
Das et al. (2009)