› 4h3d

X-ray diffraction
1.95Å resolution

1.95 Angstrom Crystal Structure of of Type I 3-Dehydroquinate Dehydratase (aroD) from Clostridium difficile with Covalent Modified Comenic Acid.

Released:
DOI: 10.2210/pdb4h3d/pdb
PDB entry 4h3d coloured by chain, front view.
PDB entry 4h3d coloured by chain, side view.
PDB entry 4h3d coloured by chain, top view.
Source organism: Clostridioides difficile 630
Entry authors: Minasov G, Light SH, Shuvalova L, Duban M-E, Dubrovska I, Winsor J, Papazisi L, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed: 
3-dehydroquinate = 3-dehydroshikimate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-dehydroquinate dehydratase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 258 amino acids
Theoretical weight: 29.19 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q186A6 (Residues: 1-255; Coverage: 100%)
Gene names: CD630_22170, aroD
Sequence domains: Type I 3-dehydroquinase
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand PGE 2 x PGE
Ligand PEG 2 x PEG
Ligand SHL 4 x SHL
Ligand ACT 3 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 60.275Å b: 138.688Å c: 66.315Å
α: 90° β: 90.01° γ: 90°
R-values:
R R work R free
0.158 0.156 0.199
Expression system: Escherichia coli BL21

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