Research workbench
Crystal structure of EPHA2/SHIP2 complex
Analyse Crystal structure of EPHA2/SHIP2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZRX
- Type
- protein
- Length
- 251 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2, ephrin type-a receptor 2
- EC
- 3.1.3.86, 2.7.10.1
- UniProt
- Q6P549, Q03145
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2, ephrin type-a receptor 2 (EC 3.1.3.86, 2.7.10.1) | protein | 126 | 67% helix, 0% strand | Q6P549, Q03145 |
| B | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2, ephrin type-a receptor 2 (EC 3.1.3.86, 2.7.10.1) | protein | 125 | 66% helix, 0% strand | Q6P549, Q03145 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.51 | 0.79 | 18 | empty |
| 2 | 84 | 0.37 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 657 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5ZRX · Crystal Structure of EphA2/SHIP2 Complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q03145 · AlphaFold monomer V2.0 prediction for ephrin type-a receptor 2 (Q03145) · a predicted model of the same protein · chain A against A, TM-score 0.64
- Q6P549 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 3,4,5-trisphosphate… · a predicted model of the same protein · chain B against A, TM-score 0.47
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 Q6P549
- Every structure of UniProt Q03145
- Elsewhere: RCSB PDB 5ZRX · PDBe 5ZRX · UniProt Q6P549 · UniProt Q03145
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