4wkg

X-ray diffraction
2.7Å resolution

The crystal structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic coop-erativity

Released:

Function and Biology Details

Reactions catalysed:
UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L-threo-pentapyranos-4-ulose + CO(2) + NADH
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinose

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-160163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional polymyxin resistance protein ArnA Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 660 amino acids
Theoretical weight: 74.39 KDa
Source organism: Escherichia coli K-12
UniProt:
  • Canonical: P77398 (Residues: 1-660; Coverage: 100%)
Gene names: JW2249, arnA, b2255, pmrI, yfbG
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P1
Unit cell:
a: 106.72Å b: 112.82Å c: 113.61Å
α: 81.92° β: 82.96° γ: 83.8°
R-values:
R R work R free
0.207 0.205 0.232