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Crystal structure of the EPHA4-EPHRINB2 complex

Analyse Crystal structure of the EPHA4-EPHRINB2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WO2
Type
protein
Length
314 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ephrin type-a receptor; Ephrin-B2
EC
2.7.10.1
UniProt
P54764, P52799
Ligands
NAG
Pockets
4 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEphrin type-a receptor (EC 2.7.10.1)protein1785% helix, 47% strandP54764
BEphrin-B2protein1368% helix, 32% strandP52799

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12890.570.7728empty
21340.420.7521empty
31010.360.7518empty
4570.360.7917empty

Interfaces

1 interface between chains.

  • A–B · 1283 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 2WO2 · Crystal Structure of the EphA4-ephrinB2 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P52799 · AlphaFold monomer V2.0 prediction for ephrin-B2 (P52799) · a predicted model of the same protein · chain B against A, TM-score 0.97
  • P54764 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 4 (P54764) · a predicted model of the same protein · chain A against A, TM-score 0.92

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