› 1osc

X-ray diffraction
2.15Å resolution

Crystal structure of rat CUTA1 at 2.15 A resolution

Released:
DOI: 10.2210/pdb1osc/pdb
PDB entry 1osc coloured by chain, front view.
PDB entry 1osc coloured by chain, side view.
PDB entry 1osc coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction.
Arnesano F, Banci L, Benvenuti M, Bertini I, Calderone V, Mangani S, Viezzoli MS
J Biol Chem 278 45999-6006 (2003)
PMID: 12949080

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-179881 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein CutA Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 126 amino acids
Theoretical weight: 13.6 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6MGD0 (Residues: 44-169; Coverage: 87%)
Gene name: Cuta
Sequence domains: CutA1 divalent ion tolerance protein
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 70.387Å b: 88.287Å c: 125.853Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.189 0.26
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Copper homeostasis.
Burkhead et al. (2009)
7 more

2 mentions without citation

A fragment-based protein interface design algorithm for symmetric assemblies.
Laniado et al. (2021)
1 more