X-ray diffraction
2.4Å resolution

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

Source organism: Deinococcus radiodurans R1
Entry authors: Bozzi AT, Zimanyi CM, Nicoludis JM, Gaudet R

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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 105.758Å b: 80.389Å c: 51.754Å
α: 90° β: 94.72° γ: 90°
R R work R free
0.239 0.237 0.279
Expression system: Escherichia coli