PDBe 1f0m

X-ray diffraction
2.2Å resolution

MONOMERIC STRUCTURE OF THE HUMAN EPHB2 SAM (STERILE ALPHA MOTIF) DOMAIN

Released:
Source organism: Homo sapiens
Primary publication:
Monomeric structure of the human EphB2 sterile alpha motif domain.
J. Biol. Chem. 274 37301-6 (1999)
PMID: 10601296

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-B receptor 2 Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.4 KDa
Source organism: Homo sapiens
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: NSLS BEAMLINE X12C
Spacegroup: P43212
Unit cell:
a: 54.837Å b: 54.837Å c: 65.545Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.243 0.264