› 1kr4

X-ray diffraction
1.4Å resolution

Structure Genomics, Protein TM1056, cutA

Released:
DOI: 10.2210/pdb1kr4/pdb
PDB entry 1kr4 coloured by chain, front view.
PDB entry 1kr4 coloured by chain, side view.
PDB entry 1kr4 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
X-ray crystal structure of CutA from Thermotoga maritima at 1.4 A resolution.
Savchenko A, Skarina T, Evdokimova E, Watson JD, Laskowski R, Arrowsmith CH, Edwards AM, Joachimiak A, Zhang RG
Proteins 54 162-5 (2004)
PMID: 14705033

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194707 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Divalent-cation tolerance protein CutA Chain: A
Molecule details ›
Chain: A
Length: 125 amino acids
Theoretical weight: 15.02 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X0E6 (Residues: 1-101; Coverage: 100%)
Gene names: TM_1056, cutA
Sequence domains: CutA1 divalent ion tolerance protein
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3
Unit cell:
a: 52.237Å b: 52.237Å c: 33.846Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.218 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
6 other articles

10 mentions without citation

Structural basis of differential neutralization of DENV-1 genotypes by an antibody that recognizes a cryptic epitope.
Austin et al. (2012)
9 more