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X-ray diffraction
2.95Å resolution

Structure of the D-Erythrose-4-Phosphate Dehydrogenase from E. coli in complex with a NAD cofactor analog (3-Chloroacetyl adenine pyridine dinucleotide) and sulfate anion

Released:
DOI: 10.2210/pdb2xf8/pdb
PDB 2xf8 coloured by chain and viewed from the front.
PDB 2xf8 coloured by chain and viewed from the side.
PDB 2xf8 coloured by chain and viewed from the top.
Source organism: Escherichia coli K-12
Entry authors: Moniot S, Didierjean C, Boschi-Muller S, Branlant G, Corbier C

Function and Biology Details

Reaction catalysed: 
D-erythrose 4-phosphate + NAD(+) + H(2)O = 4-phosphoerythronate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-erythrose-4-phosphate dehydrogenase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 338 amino acids
Theoretical weight: 37.22 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P0A9B6 (Residues: 2-339; Coverage: 100%)
Gene names: JW2894, b2927, epd, gapB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand 3CD 8 x 3CD
1 bound ligand:
Ligand SO4 16 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P1
Unit cell:
a: 96.18Å b: 111.66Å c: 135.47Å
α: 91.3° β: 96.11° γ: 88.44°
R-values:
R R work R free
0.239 0.237 0.28
Expression system: Escherichia coli K-12

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