PDBe 3kka

X-ray diffraction
2.4Å resolution

Co-crystal structure of the sam domains of EPHA1 AND EPHA2

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Yermekbayeva L, Butler-Cole C, Weigelt J, Bountra C, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

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:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ephrin type-A receptor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 82 amino acids
Theoretical weight: 9.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21709 (Residues: 911-974; Coverage: 7%)
Gene names: EPH, EPHA1, EPHT, EPHT1
Structure domains: Transcription Factor, Ets-1
Ephrin type-A receptor 2 Chains: C, D, E
Molecule details ›
Chains: C, D, E
Length: 86 amino acids
Theoretical weight: 10.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29317 (Residues: 903-971; Coverage: 7%)
Gene names: ECK, EPHA2
Structure domains: Transcription Factor, Ets-1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 57.554Å b: 56.071Å c: 107.617Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.235
Expression system: Escherichia coli