Research workbench
C-terminal SH2 domain of P120RASGAP
Analyse C-terminal SH2 domain of P120RASGAP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WAX
- Type
- protein
- Length
- 207 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS GTPase-activating protein 1
- UniProt
- P20936
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS GTPase-activating protein 1 | protein | 105 | 19% helix, 28% strand | P20936 |
| B | RAS GTPase-activating protein 1 | protein | 102 | 20% helix, 28% strand | P20936 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.46 | 0.80 | 27 | empty |
| 2 | 88 | 0.43 | 0.79 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 608 Ų buried · 13 hydrogen bonds · protein-protein
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 P20936
- Elsewhere: RCSB PDB 6WAX · PDBe 6WAX · UniProt P20936
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.