› 1jdf

X-ray diffraction
2Å resolution

Glucarate Dehydratase from E.coli N341D mutant

Released:
DOI: 10.2210/pdb1jdf/pdb
Model geometry
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PDB entry 1jdf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli.
Gulick AM, Hubbard BK, Gerlt JA, Rayment I
Biochemistry 40 10054-62 (2001)
PMID: 11513584

Function and Biology Details

Reaction catalysed: 
D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142487 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucarate dehydratase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 446 amino acids
Theoretical weight: 49.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AES2 (Residues: 1-446; Coverage: 100%)
Gene names: JW2758, b2787, gudD, ygcX
Sequence domains: Enolase C-terminal domain-like
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 4 x MG
Ligand GLR 4 x GLR
Ligand IPA 8 x IPA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 70.925Å b: 83.926Å c: 98.222Å
α: 104.11° β: 93.75° γ: 113.12°
R-values:
R R work R free
0.198 0.198 0.233
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity.
Gerlt et al. (2005)
3 more

1 mention without citation

Revisiting gap locations in amino acid sequence alignments and a proposal for a method to improve them by introducing solvent accessibility.
Hijikata et al. (2011)

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