› 3mbw

X-ray diffraction
2.81Å resolution

Crystal structure of the human ephrin A2 LBD and CRD domains in complex with ephrin A1

Released:
DOI: 10.2210/pdb3mbw/pdb
PDB entry 3mbw coloured by chain, front view.
PDB entry 3mbw coloured by chain, side view.
PDB entry 3mbw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Architecture of Eph receptor clusters.
Himanen JP, Yermekbayeva L, Janes PW, Walker JR, Xu K, Atapattu L, Rajashankar KR, Mensinga A, Lackmann M, Nikolov DB, Dhe-Paganon S
Proc Natl Acad Sci U S A 107 10860-5 (2010)
PMID: 20505120

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149074 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Ephrin type-A receptor 2 Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 36.59 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P29317 (Residues: 23-326; Coverage: 32%)
Gene names: ECK, EPHA2
Sequence domains: Ephrin receptor ligand binding domain
Structure domains:
Ephrin-A1, secreted form Chain: B
Molecule details ›
Chain: B
Length: 181 amino acids
Theoretical weight: 21.4 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P20827 (Residues: 17-171; Coverage: 82%)
Gene names: EFNA1, EPLG1, LERK1, TNFAIP4
Sequence domains: Ephrin
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
1 bound ligand:
Ligand UNX 1 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 58.265Å b: 215.787Å c: 107.263Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.226 0.272
Expression system: Spodoptera frugiperda

Quick links

Citations

61 review citations

Mechanisms of ephrin-Eph signalling in development, physiology and disease.
Kania et al. (2016)
60 more

3 mentions without citation

Architecture of Eph receptor clusters.
Himanen et al. (2010)
2 more