› 2hpr

X-ray diffraction
2Å resolution

HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR MUTANT WITH MET 51 REPLACED BY VAL AND SER 83 REPLACED BY CYS (M51V, S83C)

Released:
DOI: 10.2210/pdb2hpr/pdb
PDB entry 2hpr coloured by chain, front view.
PDB entry 2hpr coloured by chain, side view.
PDB entry 2hpr coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins.
Liao DI, Herzberg O
Structure 2 1203-16 (1994)
PMID: 7704530

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-140403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphocarrier protein HPr Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 9.07 KDa
Source organism: Bacillus subtilis
Expression system: Not provided
UniProt:
  • Canonical: P08877 (Residues: 2-88; Coverage: 99%)
Gene names: BSU13900, ptsH
Sequence domains: PTS HPr component phosphorylation site
Structure domains: HPr-like

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 47.26Å b: 47.26Å c: 61.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.145 not available not available
Expression system: Not provided

Quick links

Citations

14 citation in other articles

Progress over the first decade of CASP experiments.
Kryshtafovych et al. (2005)
13 more

7 mentions without citation

Protein-protein docking benchmark version 3.0.
Hwang et al. (2008)
6 more