› 1t3v

Solution NMR

The NMR solution structure of TM1816

Released:
DOI: 10.2210/pdb1t3v/pdb
PDB entry 1t3v coloured by chain, ensemble of 22 models, front view.
PDB entry 1t3v coloured by chain, ensemble of 22 models, side view.
PDB entry 1t3v coloured by chain, ensemble of 22 models, top view.
Source organism: Thermotoga maritima
Primary publication:
NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.
Columbus L, Peti W, Etezady-Esfarjani T, Herrmann T, Wüthrich K
Proteins 60 552-7 (2005)
PMID: 15937903

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194892 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dinitrogenase iron-molybdenum cofactor biosynthesis domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 124 amino acids
Theoretical weight: 13.65 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X2D6 (Residues: 1-124; Coverage: 100%)
Gene name: TM_1816
Sequence domains: Dinitrogenase iron-molybdenum cofactor
Structure domains: Dinitrogenase iron-molybdenum cofactor biosynthesis domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

4 mentions without citation

The anaerobe-specific orange protein complex of Desulfovibrio vulgaris hildenborough is encoded by two divergent operons coregulated by σ54 and a cognate transcriptional regulator.
Fiévet et al. (2011)
3 more