2WO3: EphA4-ephrinA2 complex

Crystal Structure of the EphA4-ephrinA2 complex. Determined by X-ray diffraction at 2.35 Å resolution. Released 27 Oct 2009.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,740
Mol. weight: 39.96 kDa
Released: 27 Oct 2009

Explore 2WO3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WO3 contains 11 α-helices and 24 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	30-35	6	1
β-strand	46-48	3	2
β-strand	55-60	6	1
β-strand	66-73	8	1
β-strand	82-85	4	2
β-strand	89-90	2	2
β-strand	97-105	9	1
β-strand	106	1	3
α-helix	108-110	3
β-strand	119	1	4
β-strand	121-129	9	2
α-helix	139-141	3
α-helix	142	1
β-strand	143-149	7	2
β-strand	154	1	3
α-helix	156-161	6
β-strand	167-173	7	1
β-strand	180-187	8	2
β-strand	190	1	4
β-strand	191-202	12	1

Chain B: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	36-40	5	5
β-strand	59-63	5	6
β-strand	68-72	5	5
α-helix	73-74	2
α-helix	77	1
α-helix	80-82	3
α-helix	83-85	3
β-strand	89-94	6	6
α-helix	96-101	6
β-strand	108-114	7	6
β-strand	125-129	5	5
β-strand	147-153	7	6
α-helix	163-164	2
β-strand	165-170	6	6
α-helix	171-173	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ephrin type-a receptor	A	protein	185	Homo sapiens	P54764 (AlphaFold model)
Ephrin-A2	B	protein	157	Homo sapiens	O43921 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2WO3_1 EPHRIN TYPE-A RECEPTOR (chains A)
ETGEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRT
DWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKID
TIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKRTKH
HHHHH

Sequence of entity 2 (B), FASTA

>2WO3_2 EPHRIN-A2 (chains B)
ETGNSDRYAVYWNRSNPRFHAGAGDDGGGYTVEVSINDYLDIYCPHYGAPLPPAERMEHY
VLYMVNGEGHASCDHRQRGFKRWECNRPAAPGGPLKFSEKFQLFTPFSLGFEFRPGHEYY
YISATPPNAVDRPCLRLKVYVRPTQETLGTKHHHHHH

Primary citation

Structural Plasticity of Eph-Receptor A4 Facilitates Cross-Class Ephrin Signalling. Bowden, T.A., Aricescu, A.R., Nettleship, J.E. et al. Structure (2009) 17:1386. DOI 10.1016/J.STR.2009.07.018 · PubMed

Other PDB entries of the same protein (UniProt P54764 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7OFV 1.43 Å, NMR-guided design of potent and selective EphA4 agonistic ligands
5JR2 1.75 Å, Crystal structure of the EphA4 LBD in complex with APYd3 peptide inhibitor
2WO1 1.85 Å, Crystal Structure of the EphA4 Ligand Binding Domain
4M4P 2.08 Å, Crystal structure of EPHA4 ectodomain
4W4Z 2.41 Å, Structure of the EphA4 LBD in complex with peptide
4W50 2.42 Å, Structure of the EphA4 LBD in complex with peptide
2WO2 2.45 Å, Crystal Structure of the EphA4-ephrinB2 complex
3GXU 2.5 Å, Crystal structure of Eph receptor and ephrin complex
9CY8 2.5 Å, Constrained b-hairpins targeting the EphA4 ligand binding domain
3CKH 2.8 Å, Crystal structure of Eph A4 receptor
4M4R 3.13 Å, Epha4 ectodomain complex with ephrin a5
4BK4 3.65 Å, crystal structure of the human EphA4 ectodomain

Browse structure collections

About this viewer

MolViewer shows 2WO3 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.