Research workbench
The small G protein RAP2 in a non catalytic complex with GTP
Analyse The small G protein RAP2 in a non catalytic complex with GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RAP
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (G protein RAP2A)
- UniProt
- P10114
- Ligands
- GTP, MG
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R, S | Protein (G protein RAP2A) | protein | 167 | 41% helix, 27% strand | P10114 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains R, S
- MG · Magnesium ion · metal · 2 copies · chains R, S
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.59 | 0.79 | 36 | empty |
| 2 | 179 | 0.56 | 0.80 | 31 | MG, GTP |
| 3 | 143 | 0.53 | 0.80 | 30 | MG, GTP |
| 4 | 67 | 0.39 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- R–S · 400 Ų buried · 0 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 P10114
- Elsewhere: RCSB PDB 3RAP · PDBe 3RAP · UniProt P10114
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