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Crystal structure of eph A4 receptor
Analyse Crystal structure of eph A4 receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CKH
- Type
- protein
- Length
- 337 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ephrin type-a receptor 4
- EC
- 2.7.10.1
- UniProt
- P54764
- Pockets
- 5 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin type-a receptor 4 (EC 2.7.10.1) | protein | 170 | 7% helix, 45% strand | P54764 |
| B | Ephrin type-a receptor 4 (EC 2.7.10.1) | protein | 167 | 5% helix, 46% strand | P54764 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.61 | 0.83 | 37 | empty |
| 2 | 100 | 0.44 | 0.78 | 14 | empty |
| 3 | 143 | 0.44 | 0.75 | 17 | empty |
| 4 | 139 | 0.41 | 0.74 | 22 | empty |
| 5 | 52 | 0.41 | 0.82 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 651 Ų buried · 10 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 3CKH · PDBe 3CKH · UniProt P54764
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