› 1sj5

X-ray diffraction
2.8Å resolution

Crystal structure of a duf151 family protein (tm0160) from thermotoga maritima at 2.8 A resolution

Released:
DOI: 10.2210/pdb1sj5/pdb
PDB entry 1sj5 coloured by chain, front view.
PDB entry 1sj5 coloured by chain, side view.
PDB entry 1sj5 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171.
Spraggon G, Pantazatos D, Klock HE, Wilson IA, Woods VL, Lesley SA
Protein Sci 13 3187-99 (2004)
PMID: 15557262

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BFN domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.45 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WY07 (Residues: 1-145; Coverage: 80%)
Gene name: TM_0160
Sequence domains: Bifunctional nuclease domain
Structure domains: Bifunctional nuclease domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 44.001Å b: 52.136Å c: 73.33Å
α: 90° β: 97.64° γ: 90°
R-values:
R R work R free
0.219 0.216 0.276
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
3 more

1 mention without citation

On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171.
Spraggon et al. (2004)