› 1pfh

Solution NMR

THE PHOSPHORYLATED FORM OF THE HISTIDINE-CONTAINING PHOSPHOCARRIER PROTEIN HPR

Released:
DOI: 10.2210/pdb1pfh/pdb
PDB entry 1pfh coloured by chain, ensemble of 20 models, front view.
PDB entry 1pfh coloured by chain, ensemble of 20 models, side view.
PDB entry 1pfh coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.
van Nuland NA, Boelens R, Scheek RM, Robillard GT
J Mol Biol 246 180-93 (1995)
PMID: 7853396

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141942 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphocarrier protein HPr Chain: A
Molecule details ›
Chain: A
Length: 85 amino acids
Theoretical weight: 9.21 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0AA04 (Residues: 1-85; Coverage: 100%)
Gene names: JW2408, b2415, hpr, ptsH
Sequence domains: PTS HPr component phosphorylation site
Structure domains: HPr-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand HIP 1 x HIP

Experiments and Validation Details

Entry percentile scores

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Citations

6 review citations

Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system.
Robillard et al. (1999)
5 more

3 mentions without citation

The many ways that nature has exploited the unusual structural and chemical properties of phosphohistidine for use in proteins.
Kalagiri et al. (2021)
2 more