› 5vxa

X-ray diffraction
2.1Å resolution

Structure of the human Mesh1-NADPH complex

Released:
DOI: 10.2210/pdb5vxa/pdb
PDB entry 5vxa coloured by chain, front view.
PDB entry 5vxa coloured by chain, side view.
PDB entry 5vxa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
MESH1 is a cytosolic NADPH phosphatase that regulates ferroptosis.
Ding CC, Rose J, Sun T, Wu J, Chen PH, Lin CC, Yang WH, Chen KY, Lee H, Xu E, Tian S, Akinwuntan J, Zhao J, Guan Z, Zhou P, Chi JT
Nat Metab 2 270-277 (2020)
PMID: 32462112

Function and Biology Details

Reaction catalysed: 
Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 180 amino acids
Theoretical weight: 20.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8N4P3 (Residues: 1-179; Coverage: 100%)
Gene names: HDDC3, MESH1
Sequence domains: HD domain
Structure domains: Hypothetical protein af1432

Ligands and Environments

6 bound ligands:
Ligand ZN 2 x ZN
Ligand NDP 2 x NDP
Ligand EDO 3 x EDO
Ligand BME 2 x BME
Ligand NA 1 x NA
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 47.78Å b: 80.37Å c: 114.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.165 0.206
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Ferroptosis: molecular mechanisms and health implications.
Tang et al. (2021)
24 more

6 mentions without citation

Metazoan stringent-like response mediated by MESH1 phenotypic conservation via distinct mechanisms.
Mestre et al. (2022)
5 more