3zcc

X-ray diffraction
1.25Å resolution

High resolution structure of the asymmetric R333G Hamp-Dhp mutant

Released:
Entry authors: Zeth K, Muench C, Ferris H

Function and Biology Details

Reaction catalysed:
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-128062 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HAMP domain-containing protein; Sensor histidine kinase EnvZ Chains: A, B
Molecule details ›
Chains: A, B
Length: 114 amino acids
Theoretical weight: 12.75 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: O28769 (Residues: 278-327; Coverage: 15%)
  • Canonical: P0AEJ4 (Residues: 229-288; Coverage: 13%)
Gene names: AF_1503, JW3367, b3404, envZ, ompB, perA, tpo
Sequence domains:
Structure domains: Helix Hairpins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 36.06Å b: 57.46Å c: 52.34Å
α: 90° β: 107.84° γ: 90°
R-values:
R R work R free
0.19 0.19 0.204
Expression system: Escherichia coli