› 2x86

X-ray diffraction
2.8Å 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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159258 (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, K, L, M, N, O, P, Q, R, S, T
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Length: 357 amino acids
Theoretical weight: 39.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P67911 (Residues: 1-310; Coverage: 100%)
Gene names: ECs4497, Z5046, hldD, rfaD
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 20 x NAP
2 bound ligands:
Ligand ADP 20 x ADP
Ligand BMA 19 x BMA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 138.074Å b: 162.458Å c: 185.027Å
α: 90° β: 101.45° γ: 90°
R-values:
R R work R free
0.253 0.252 0.272
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

The crystal structure of the Y140F mutant of ADP-L-glycero-D-manno-heptose 6-epimerase bound to ADP-beta-D-mannose suggests a one base mechanism.
Kowatz et al. (2010)
1 more