› 1sgg

Solution NMR

THE SOLUTION STRUCTURE OF SAM DOMAIN FROM THE RECEPTOR TYROSINE KINASE EPHB2, NMR, 10 STRUCTURES

Released:
DOI: 10.2210/pdb1sgg/pdb
PDB entry 1sgg coloured by chain, ensemble of 10 models, front view.
PDB entry 1sgg coloured by chain, ensemble of 10 models, side view.
PDB entry 1sgg coloured by chain, ensemble of 10 models, top view.
Source organism: Gallus gallus
Primary publication:
Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites.
Smalla M, Schmieder P, Kelly M, Ter Laak A, Krause G, Ball L, Wahl M, Bork P, Oschkinat H
Protein Sci 8 1954-61 (1999)
PMID: 10548040

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151262 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
EphB2/CTF2 Chain: A
Molecule details ›
Chain: A
Length: 75 amino acids
Theoretical weight: 8.54 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P28693 (Residues: 924-998; Coverage: 8%)
Gene names: CEK5, EPHB2
Sequence domains: SAM domain (Sterile alpha motif)
Structure domains: Transcription Factor, Ets-1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

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Citations

14 review citations

Mechanisms and functions of Eph and ephrin signalling.
Kullander et al. (2002)
13 more