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Structure of wild type mus musculus rheb bound to GTP
Analyse Structure of wild type mus musculus rheb bound to GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O25
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding protein rheb
- UniProt
- Q921J2
- Ligands
- GTP, MG
- Pockets
- 7 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | GTP-binding protein rheb | protein | 167 | 34% helix, 26% strand | Q921J2 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.53 | 0.79 | 32 | MG, GTP |
| 2 | 115 | 0.49 | 0.80 | 25 | GTP, MG |
| 3 | 141 | 0.47 | 0.77 | 22 | empty |
| 4 | 110 | 0.39 | 0.74 | 18 | empty |
| 5 | 63 | 0.32 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 425 Ų buried · 7 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 Q921J2
- Elsewhere: RCSB PDB 4O25 · PDBe 4O25 · UniProt Q921J2
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