› 2ka5

Solution NMR

NMR Structure of the protein TM1081

Released:
DOI: 10.2210/pdb2ka5/pdb
PDB entry 2ka5 coloured by chain, ensemble of 20 models, front view.
PDB entry 2ka5 coloured by chain, ensemble of 20 models, side view.
PDB entry 2ka5 coloured by chain, ensemble of 20 models, top view.
Source organism: Thermotoga maritima
Primary publication:
Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.
Serrano P, Pedrini B, Geralt M, Jaudzems K, Mohanty B, Horst R, Herrmann T, Elsliger MA, Wilson IA, Wüthrich K
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 1393-405 (2010)
PMID: 20944236

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-194714 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative anti-sigma factor antagonist TM_1081 Chain: A
Molecule details ›
Chain: A
Length: 125 amino acids
Theoretical weight: 14.45 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0H0 (Residues: 1-113; Coverage: 100%)
Gene name: TM_1081
Sequence domains: STAS domain
Structure domains: STAS domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 83%
Refinement method: molecular dynamics
Expression system: Escherichia coli

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Citations

1 review citation

γ-Glutamylamines and neurodegenerative diseases.
Jeitner et al. (2013)
6 other articles

1 mention without citation

Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.
Serrano et al. (2010)