2WO1: EphA4 Ligand Binding Domain

Crystal Structure of the EphA4 Ligand Binding Domain. Determined by X-ray diffraction at 1.85 Å resolution. Released 27 Oct 2009.

Method: X-ray diffraction
Resolution: 1.85 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,253
Mol. weight: 43.23 kDa
Ligands: POL
Released: 27 Oct 2009

Explore 2WO1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WO1 contains 7 α-helices and 28 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, 13 β-strands

Element	Residues	Length	Sheet
β-strand	28-35	8	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
β-strand	89-90	2	2
β-strand	97-105	9	1
α-helix	108-110	3
β-strand	121-129	9	2
α-helix	139-141	3
β-strand	143-149	7	2
β-strand	154-157	4	1
β-strand	164-173	10	1
β-strand	180-187	8	2
β-strand	191-204	14	1
α-helix	206-208	3

Chain B: 3 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	30-35	6	3
α-helix	36-38	3
β-strand	46-48	3	4
β-strand	55-60	6	3
β-strand	66-73	8	3
β-strand	82-85	4	4
β-strand	89-90	2	4
β-strand	97-105	9	3
α-helix	108-110	3
β-strand	119	1	5
β-strand	121-129	9	4
α-helix	139-141	3
β-strand	143-149	7	4
β-strand	154-158	5	3
β-strand	163-173	11	3
β-strand	180-187	8	4
β-strand	190	1	5
β-strand	191-202	12	3

Molecules and chains

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

Sequence of entity 1 (A, B), FASTA

>2WO1_1 EPHRIN TYPE-A RECEPTOR (chains A, B)
ETGEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRT
DWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKID
TIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKRTKH
HHHHH

Ligands and cofactors

ID	Name	Formula	Copies
POL	N-propanol	C3 H8 O	5

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
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
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

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