4kfg

X-ray diffraction
1.6Å resolution

The DNA Gyrase B ATP binding domain of Escherichia coli in complex with a small molecule inhibitor.

Released:
Source organism: Escherichia coli K-12
Entry authors: Bensen DC, Akers-Rodriguez S, Lam T, Tari LW

Function and Biology Details

Reaction catalysed:
ATP-dependent breakage, passage and rejoining of double-stranded DNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA gyrase subunit B Chains: A, B
Molecule details ›
Chains: A, B
Length: 215 amino acids
Theoretical weight: 23.85 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AES6 (Residues: 15-220; Coverage: 26%)
Gene names: JW5625, acrB, b3699, cou, gyrB, himB, hisU, nalC, parA, pcbA
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: P21
Unit cell:
a: 47.894Å b: 82.477Å c: 53.74Å
α: 90° β: 100.16° γ: 90°
R-values:
R R work R free
0.194 0.192 0.221
Expression system: Escherichia coli BL21(DE3)