› 8qay

X-ray diffraction
2.2Å resolution

Medicago truncatula HISN5 (IGPD) in complex with MN, FMT, ACT, CIT, EDO, SO4

Released:
DOI: 10.2210/pdb8qay/pdb
PDB entry 8qay coloured by chain, front view.
PDB entry 8qay coloured by chain, side view.
PDB entry 8qay coloured by chain, top view.
Source organism: Medicago truncatula
Primary publication:
Targeting imidazole-glycerol phosphate dehydratase in plants: novel approach for structural and functional studies, and inhibitor blueprinting.
Witek W, Sliwiak J, Rawski M, Ruszkowski M
Front Plant Sci 15 1343980 (2024)
PMID: 38559763

Function and Biology Details

Reaction catalysed: 
D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100426 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazoleglycerol-phosphate dehydratase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 206 amino acids
Theoretical weight: 22.57 KDa
Source organism: Medicago truncatula
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A072VQG6 (Residues: 71-275; Coverage: 75%)
Gene names: 25485215, MTR_1g103820
Sequence domains: Imidazoleglycerol-phosphate dehydratase

Ligands and Environments

7 bound ligands:
Ligand FMT 25 x FMT
Ligand CIT 2 x CIT
Ligand MN 16 x MN
Ligand EDO 10 x EDO
Ligand SO4 2 x SO4
Ligand NA 1 x NA
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU PhotonJet-R
Spacegroup: R3
Unit cell:
a: 137.6Å b: 137.6Å c: 265.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.189 0.231
Expression system: Escherichia coli

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