X-ray diffraction
2.36Å resolution

Crystal structure of the Deinococcus radiodurans Nramp/MntH divalent transition metal transporter in the outward-open, apo conformation


Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Divalent metal cation transporter MntH Chain: A
Molecule details ›
Chain: A
Length: 412 amino acids
Theoretical weight: 44.61 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli
  • Canonical: Q9RTP8 (Residues: 35-436; Coverage: 92%)
Gene names: DR_1709, mntH
Sequence domains: Natural resistance-associated macrophage protein

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 101.919Å b: 75.508Å c: 53.151Å
α: 90° β: 98.07° γ: 90°
R R work R free
0.249 0.244 0.299
Expression system: Escherichia coli