› 2k1l

Solution NMR

NMR structures of dimeric transmembrane domain of the receptor tyrosine kinase EphA1 in lipid bicelles at pH 6.3

Released:
DOI: 10.2210/pdb2k1l/pdb
PDB entry 2k1l coloured by chain, ensemble of 12 models, front view.
PDB entry 2k1l coloured by chain, ensemble of 12 models, side view.
PDB entry 2k1l coloured by chain, ensemble of 12 models, top view.
Source organism: Homo sapiens
Primary publication:
Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1.
Bocharov EV, Mayzel ML, Volynsky PE, Goncharuk MV, Ermolyuk YS, Schulga AA, Artemenko EO, Efremov RG, Arseniev AS
J Biol Chem 283 29385-95 (2008)
PMID: 18728013

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-A receptor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 38 amino acids
Theoretical weight: 3.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21709 (Residues: 536-573; Coverage: 4%)
Gene names: EPH, EPHA1, EPHT, EPHT1
Sequence domains: Ephrin type-A receptor 2 transmembrane 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

17 review citations

The magic of bicelles lights up membrane protein structure.
Dürr et al. (2012)
16 more

12 mentions without citation

Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?
Hubert et al. (2010)
11 more