Research workbench
Ligand recognition by a-class eph receptors: crystal structures of the EPHA2 ligand-binding domain and the EPHA2/EPHRIN-A1 complex
Analyse Ligand recognition by a-class eph receptors: crystal structures of the EPHA2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HEI
- Type
- protein
- Length
- 2,448 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ephrin type-a receptor 2; Ephrin-A1
- EC
- 2.7.10.1
- UniProt
- P29317, P20827
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O | Ephrin type-a receptor 2 (EC 2.7.10.1) | protein | 174 | 8% helix, 47% strand | P29317 |
| B, D, F, H, J, L, N, P | Ephrin-A1 | protein | 132 | 11% helix, 33% strand | P20827 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 838 | 0.83 | 0.86 | 113 | empty |
| 2 | 1163 | 0.78 | 0.80 | 97 | empty |
| 3 | 1018 | 0.77 | 0.79 | 105 | empty |
| 4 | 1043 | 0.77 | 0.79 | 108 | empty |
| 5 | 278 | 0.68 | 0.84 | 41 | empty |
Interfaces
24 interfaces between chains.
- O–P · 1182 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 1171 Ų buried · 11 hydrogen bonds · protein-protein
- G–H · 1166 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1162 Ų buried · 12 hydrogen bonds · protein-protein
- K–L · 1155 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 disulfide (disulfide).
Compared structures
- 3HEI · Ligand Recognition by A-Class Eph Receptors: Crystal Structures of the EphA2… · the same entry in another collection · chain J against J, TM-score 1.00
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 P29317
- Every structure of UniProt P20827
- Elsewhere: RCSB PDB 3HEI · PDBe 3HEI · UniProt P29317 · UniProt P20827
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.