› 4ki7

X-ray diffraction
2.8Å resolution

Design and structural analysis of aromatic inhibitors of type II dehydroquinase from Mycobacterium tuberculosis - compound 41c [3-hydroxy-5-(3-nitrophenoxy)benzoic acid]

Released:
DOI: 10.2210/pdb4ki7/pdb
PDB entry 4ki7 coloured by chain, front view.
PDB entry 4ki7 coloured by chain, side view.
PDB entry 4ki7 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Design and structural analysis of aromatic inhibitors of type II dehydroquinase from Mycobacterium tuberculosis.
Howard NI, Dias MV, Peyrot F, Chen L, Schmidt MF, Blundell TL, Abell C
ChemMedChem 10 116-33 (2015)
PMID: 25234229

Function and Biology Details

Reaction catalysed: 
3-dehydroquinate = 3-dehydroshikimate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dodecamer (preferred)
homo 24-mer
Assembly name:
PDBe Complex ID:
PDB-CPX-162016 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-dehydroquinate dehydratase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 153 amino acids
Theoretical weight: 16.58 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WPX7 (Residues: 1-147; Coverage: 100%)
Gene names: MTCY159.19, Rv2537c, aroD, aroQ
Sequence domains: Dehydroquinase class II
Structure domains: Dehydroquinase, class II

Ligands and Environments

1 bound ligand:
Ligand 1R2 22 x 1R2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 96.74Å b: 139.69Å c: 143.81Å
α: 90° β: 96.43° γ: 90°
R-values:
R R work R free
0.193 0.188 0.278
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Reducing the Flexibility of Type II Dehydroquinase for Inhibition: A Fragment-Based Approach and Molecular Dynamics Study.
Peón et al. (2017)

1 mention without citation

π-Hole Interactions Involving Nitro Aromatic Ligands in Protein Structures.
Bauzá et al. (2019)