› 1eq2

X-ray diffraction
2Å resolution

THE CRYSTAL STRUCTURE OF ADP-L-GLYCERO-D-MANNOHEPTOSE 6-EPIMERASE

Released:
DOI: 10.2210/pdb1eq2/pdb
PDB entry 1eq2 coloured by chain, front view.
PDB entry 1eq2 coloured by chain, side view.
PDB entry 1eq2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist.
Deacon AM, Ni YS, Coleman WG, Ealick SE
Structure 8 453-62 (2000)
PMID: 10896473

Function and Biology Details

Reaction catalysed: 
ADP-D-glycero-D-manno-heptose = ADP-L-glycero-D-manno-heptose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159257 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-L-glycero-D-manno-heptose-6-epimerase Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 310 amino acids
Theoretical weight: 34.94 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P67910 (Residues: 1-310; Coverage: 100%)
Gene names: JW3594, b3619, hldD, htrM, rfaD, waaD
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 10 x NAP
1 bound ligand:
Ligand ADQ 10 x ADQ
1 modified residue:
Ligand CSO 10 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21
Unit cell:
a: 99.46Å b: 109.76Å c: 181.54Å
α: 90° β: 91.04° γ: 90°
R-values:
R R work R free
0.217 0.212 0.262
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Advances in multiple wavelength anomalous diffraction crystallography.
Ealick SE. (2000)
2 more

7 mentions without citation

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
6 more