› 2fsu

X-ray diffraction
1.7Å resolution

Crystal Structure of the PhnH Protein from Escherichia Coli

Released:
DOI: 10.2210/pdb2fsu/pdb
PDB entry 2fsu coloured by chain, front view.
PDB entry 2fsu coloured by chain, side view.
PDB entry 2fsu coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of PhnH: an essential component of carbon-phosphorus lyase in Escherichia coli.
Adams MA, Luo Y, Hove-Jensen B, He SM, van Staalduinen LM, Zechel DL, Jia Z
J Bacteriol 190 1072-83 (2008)
PMID: 17993513

Function and Biology Details

Reaction catalysed: 
ATP + methylphosphonate = alpha-D-ribose 1-methylphosphonate 5-triphosphate + adenine
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-147798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH Chain: A
Molecule details ›
Chain: A
Length: 210 amino acids
Theoretical weight: 23.11 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P16686 (Residues: 1-194; Coverage: 100%)
Gene names: JW4061, b4100, phnH
Sequence domains: Bacterial phosphonate metabolism protein (PhnH)
Structure domains: Bacterial phosphonate metabolism protein PhnH

Ligands and Environments

2 bound ligands:
Ligand NA 4 x NA
Ligand ACT 1 x ACT
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: C2221
Unit cell:
a: 53.02Å b: 87.418Å c: 75.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.248

Quick links

Citations

4 review citations

Global regulation by the seven-component Pi signaling system.
Hsieh et al. (2010)
3 more

5 mentions without citation

Crystal structure of PhnH: an essential component of carbon-phosphorus lyase in Escherichia coli.
Adams et al. (2008)
4 more