› 1qr5

Solution NMR

SOLUTION STRUCTURE OF HISTIDINE CONTAINING PROTEIN (HPR) FROM STAPHYLOCOCCUS CARNOSUS

Released:
DOI: 10.2210/pdb1qr5/pdb
PDB entry 1qr5 coloured by chain, ensemble of 10 models, front view.
PDB entry 1qr5 coloured by chain, ensemble of 10 models, side view.
PDB entry 1qr5 coloured by chain, ensemble of 10 models, top view.
Source organism: Staphylococcus carnosus
Primary publication:
15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure.
Kalbitzer HR, Görler A, Li H, Dubovskii PV, Hengstenberg W, Kowolik C, Yamada H, Akasaka K
Protein Sci 9 693-703 (2000)
PMID: 10794411

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-150005 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphocarrier protein HPr Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.52 KDa
Source organism: Staphylococcus carnosus
Expression system: Escherichia coli
UniProt:
  • Canonical: P23534 (Residues: 1-88; Coverage: 100%)
Gene name: 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: RESTRAINED MD
Expression system: Escherichia coli

Quick links

Citations

1 review citation

High-pressure protein crystallography and NMR to explore protein conformations.
Collins et al. (2011)
24 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)