Research workbench
The phosphatase and C2 domains of human SHIP1
Analyse The phosphatase and C2 domains of human SHIP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IBD
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
- EC
- 3.1.3.86
- UniProt
- Q92835
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) | protein | 448 | 17% helix, 38% strand | Q92835 |
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 | 282 | 0.66 | 0.82 | 42 | empty |
| 2 | 96 | 0.46 | 0.80 | 21 | empty |
| 3 | 130 | 0.39 | 0.75 | 27 | empty |
| 4 | 63 | 0.31 | 0.75 | 17 | empty |
| 5 | 53 | 0.28 | 0.75 | 17 | empty |
Compared structures
- 6IBD · The Phosphatase and C2 domains of Human SHIP1 · the same entry in another collection · chain A against A, 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 Q92835
- Elsewhere: RCSB PDB 6IBD · PDBe 6IBD · UniProt Q92835
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