2WO2: EphA4-ephrinB2 complex

Crystal Structure of the EphA4-ephrinB2 complex. Determined by X-ray diffraction at 2.45 Å resolution. Released 27 Oct 2009.

Method: X-ray diffraction
Resolution: 2.45 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,596
Mol. weight: 39.2 kDa
Ligands: NAG
Released: 27 Oct 2009

Explore 2WO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WO2 contains 10 α-helices and 27 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: 6 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	30-35	6	1
α-helix	36-38	3
β-strand	46-48	3	2
β-strand	55-60	6	1
β-strand	66-73	8	1
β-strand	82-85	4	2
α-helix	86-88	3
β-strand	89-90	2	2
β-strand	97-105	9	1
β-strand	106	1	3
α-helix	108-110	3
α-helix	117-119	3
β-strand	121-129	9	2
α-helix	139-141	3
β-strand	143-149	7	2
β-strand	154	1	3
α-helix	162-163	2
β-strand	167-173	7	1
β-strand	180-187	8	2
β-strand	191-202	12	1

Chain B: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	29	1	4
α-helix	30-32	3
β-strand	33-34	2	4
β-strand	48-50	3	5
α-helix	52-53	2
β-strand	57-61	5	4
β-strand	75	1	6
β-strand	76-81	6	5
α-helix	83-88	6
β-strand	90	1	7
β-strand	97-101	5	5
β-strand	109-113	5	4
β-strand	130-135	6	5
β-strand	140	1	6
β-strand	149	1	7
α-helix	151-155	5
β-strand	159-164	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ephrin type-a receptor	A	protein	185	Homo sapiens	P54764 (AlphaFold model)
Ephrin-B2	B	protein	153	Homo sapiens	P52799 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2WO2_1 EPHRIN TYPE-A RECEPTOR (chains A)
ETGEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRT
DWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKID
TIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKRTKH
HHHHH

Sequence of entity 2 (B), FASTA

>2WO2_2 EPHRIN-B2 (chains B)
ETGSIVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDK
DQADRCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLE
GLDNQEGGVCQTRAMKILMKVGQDGTKHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

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
2WO3 2.35 Å, Crystal Structure of the EphA4-ephrinA2 complex
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
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

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