› 2roe

Solution NMR

Solution structure of thermus thermophilus HB8 TTHA1718 protein in vitro

Released:
DOI: 10.2210/pdb2roe/pdb
PDB entry 2roe coloured by chain, ensemble of 20 models, front view.
PDB entry 2roe coloured by chain, ensemble of 20 models, side view.
PDB entry 2roe coloured by chain, ensemble of 20 models, top view.
Source organism: Thermus thermophilus
Primary publication:
Protein structure determination in living cells by in-cell NMR spectroscopy.
Sakakibara D, Sasaki A, Ikeya T, Hamatsu J, Hanashima T, Mishima M, Yoshimasu M, Hayashi N, Mikawa T, Wälchli M, Smith BO, Shirakawa M, Güntert P, Ito Y
Nature 458 102-5 (2009)
PMID: 19262674

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177881 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HMA domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 66 amino acids
Theoretical weight: 7.05 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SHL2 (Residues: 1-66; Coverage: 100%)
Gene name: TTHA1718
Sequence domains: Heavy-metal-associated domain
Structure domains: Alpha-Beta Plaits

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

52 review citations

Protein folding and modification in the mammalian endoplasmic reticulum.
Braakman et al. (2011)
51 more

4 mentions without citation

Physicochemical code for quinary protein interactions in Escherichia coli.
Mu et al. (2017)
3 more