PDBe 1b4f

X-ray diffraction
1.95Å resolution

OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN

Released:
Source organism: Homo sapiens
Primary publication:
Oligomeric structure of the human EphB2 receptor SAM domain.
Science 283 833-6 (1999)
PMID: 9933164

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 16-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-B receptor 2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 82 amino acids
Theoretical weight: 9.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P29323 (Residues: 905-985; Coverage: 8%)
  • Best match: P29323-2 (Residues: 905-986)
Gene names: DRT, EPHB2, EPHT3, EPTH3, ERK, HEK5, TYRO5
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
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P41
Unit cell:
a: 73.897Å b: 73.897Å c: 104.547Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.273
Expression system: Escherichia coli BL21