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Crystal structure of the EPHA4 ligand binding domain
Analyse Crystal structure of the EPHA4 ligand binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WO1
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ephrin type-a receptor
- EC
- 2.7.10.1
- UniProt
- P54764
- Pockets
- 7 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin type-a receptor (EC 2.7.10.1) | protein | 180 | 5% helix, 51% strand | P54764 |
| B | Ephrin type-a receptor (EC 2.7.10.1) | protein | 176 | 5% helix, 52% strand | P54764 |
Ligands and binding sites
- POL · N-propanol · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.59 | 0.84 | 35 | POL |
| 2 | 208 | 0.55 | 0.78 | 37 | empty |
| 3 | 247 | 0.52 | 0.76 | 37 | POL |
| 4 | 113 | 0.43 | 0.77 | 17 | empty |
| 5 | 62 | 0.41 | 0.80 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 876 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P54764
- Elsewhere: RCSB PDB 2WO1 · PDBe 2WO1 · UniProt P54764
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