MolNFT v1 · #121827 · protein
Structure of F285S, a cancer-associated mutation of the oncogenic phosphatase SHP2
5I6V · Tyrosine-protein phosphatase non-receptor type 11: “Structure of F285S, a cancer-associated mutation of the oncogenic phosphatase SHP2”. X-ray diffraction, 11 pockets (best druggability 0.68). MolNFT v1 #121827 on GenesisL1: 3D…
- PDB
- 5I6V
- Type
- protein
- Length
- 984 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 11
- EC
- 3.1.3.48
- UniProt
- Q06124
- Pockets
- 11 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) | protein | 488 | 30% helix, 27% strand | Q06124 |
| B | Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) | protein | 496 | 30% helix, 26% strand | Q06124 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 838 | 0.68 | 0.74 | 93 | GOL |
| 2 | 252 | 0.58 | 0.79 | 28 | empty |
| 3 | 270 | 0.57 | 0.78 | 28 | empty |
| 4 | 266 | 0.51 | 0.74 | 38 | empty |
| 5 | 118 | 0.41 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 673 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5I6V · Structure of F285S, a Cancer-Associated Mutation of the Oncogenic Phosphatase SHP2 · 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 Q06124
- Elsewhere: RCSB PDB 5I6V · PDBe 5I6V · UniProt Q06124
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