› 2los

Solution NMR

Backbone structure of human membrane protein TMEM14C

Released:
DOI: 10.2210/pdb2los/pdb
PDB entry 2los coloured by chain, ensemble of 20 models, front view.
PDB entry 2los coloured by chain, ensemble of 20 models, side view.
PDB entry 2los coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Facile backbone structure determination of human membrane proteins by NMR spectroscopy.
Klammt C, Maslennikov I, Bayrhuber M, Eichmann C, Vajpai N, Chiu EJ, Blain KY, Esquivies L, Kwon JH, Balana B, Pieper U, Sali A, Slesinger PA, Kwiatkowski W, Riek R, Choe S
Nat Methods 9 834-9 (2012)
PMID: 22609626

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192806 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transmembrane protein 14C Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 12.61 KDa
Source organism: Homo sapiens
Expression system: CELL-FREE SYNTHESIS
UniProt:
  • Canonical: Q9P0S9 (Residues: 1-112; Coverage: 100%)
Gene names: C6orf53, HSPC194, TMEM14C
Sequence domains: Transmembrane proteins 14C
Structure domains: Transmembrane protein 14-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 41%
Refinement method: torsion angle dynamics
Expression system: CELL-FREE SYNTHESIS

Quick links

Citations

13 review citations

Computational modeling of membrane proteins.
Koehler Leman et al. (2015)
12 more

3 mentions without citation

Advances in NMR structures of integral membrane proteins.
Maslennikov et al. (2013)
2 more