MolNFT v1 · #36125 · protein
Crystal structure of RAB30 in complex with a GTP analogue
2EW1 · RAS-related protein rab-30: “Crystal structure of RAB30 in complex with a GTP analogue”. X-ray diffraction, 2 ligands (GNP, MG), 2 pockets (best druggability 0.42). MolNFT v1 #36125 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2EW1
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related protein rab-30
- UniProt
- Q15771
- Ligands
- GNP, MG
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related protein rab-30 | protein | 171 | 40% helix, 27% strand | Q15771 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
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 | 100 | 0.42 | 0.78 | 25 | MG, GNP |
| 2 | 52 | 0.28 | 0.74 | 13 | empty |
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 Q15771
- Elsewhere: RCSB PDB 2EW1 · PDBe 2EW1 · UniProt Q15771
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