› 1mqb

X-ray diffraction
2.3Å resolution

Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase

Released:
DOI: 10.2210/pdb1mqb/pdb
PDB entry 1mqb coloured by chain, front view.
PDB entry 1mqb coloured by chain, side view.
PDB entry 1mqb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography.
Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA
Structure 10 1659-67 (2002)
PMID: 12467573

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ephrin type-A receptor 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 333 amino acids
Theoretical weight: 37.78 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P29317 (Residues: 596-900; Coverage: 32%)
Gene names: ECK, EPHA2
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ANP 2 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P3221
Unit cell:
a: 72.127Å b: 72.127Å c: 241.623Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.237 0.236 0.288
Expression system: Spodoptera frugiperda

Quick links

Citations

25 review citations

Focal adhesion kinase: in command and control of cell motility.
Mitra et al. (2005)
24 more

12 mentions without citation

A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinases.
Wiesner et al. (2006)
11 more