› 2x6t

X-ray diffraction
2.36Å resolution

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159256 (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: 357 amino acids
Theoretical weight: 39.89 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
4 bound ligands:
Ligand GOL 10 x GOL
Ligand ADP 10 x ADP
Ligand BMA 10 x BMA
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 341.993Å b: 60.787Å c: 191.789Å
α: 90° β: 91.41° γ: 90°
R-values:
R R work R free
0.19 0.189 0.209
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
1 more