› 1qfr

Solution NMR

NMR SOLUTION STRUCTURE OF PHOSPHOCARRIER PROTEIN HPR FROM ENTEROCOCCUS FAECALIS

Released:
DOI: 10.2210/pdb1qfr/pdb
PDB entry 1qfr coloured by chain, ensemble of 16 models, front view.
PDB entry 1qfr coloured by chain, ensemble of 16 models, side view.
PDB entry 1qfr coloured by chain, ensemble of 16 models, top view.
Source organism: Enterococcus faecalis
Primary publication:
Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution.
Maurer T, Döker R, Görler A, Hengstenberg W, Kalbitzer HR
Eur J Biochem 268 635-44 (2001)
PMID: 11168402

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139608 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphocarrier protein HPr Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 9.46 KDa
Source organism: Enterococcus faecalis
UniProt:
  • Canonical: P07515 (Residues: 1-88; Coverage: 100%)
Gene names: EF_0709, ptsH
Sequence domains: PTS HPr component phosphorylation site
Structure domains: HPr-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: ANGULAR SPACE SIMULATED ANNEALING

Quick links

Citations

1 review citation

CcpA-dependent carbon catabolite repression in bacteria.
Warner et al. (2003)
11 other articles

1 mention without citation

A restraint molecular dynamics and simulated annealing approach for protein homology modeling utilizing mean angles.
Möglich et al. (2005)