4irm

X-ray diffraction
3.5Å resolution

Crystal structure of mntc r116a mutant exhibits flexibility in the c-terminal domain

Released:
Source organism: Synechocystis sp. PCC 6803
Primary publication:
Arginine 116 stabilizes the entrance to the metal ion-binding site of the MntC protein.
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 237-42 (2013)
PMID: 23519795

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181255 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mn transporter MntC Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 330 amino acids
Theoretical weight: 36.01 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q79EF9 (Residues: 1-330; Coverage: 100%)
Gene name: mntC
Sequence domains: Zinc-uptake complex component A periplasmic
Structure domains: Nitrogenase molybdenum iron protein domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P3121
Unit cell:
a: 128.4Å b: 128.4Å c: 90.51Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.294 0.294 0.305
Expression system: Escherichia coli BL21