MolNFT v1 · #166966 · protein
Crystal structure of rhoa-GDP with novel switch I conformation
6V6U · Transforming protein rhoa: “Crystal structure of rhoa-GDP with novel switch I conformation”. X-ray diffraction, 2 ligands (GDP, MG), 2 pockets (best druggability 0.51). MolNFT v1 #166966 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6V6U
- Type
- protein
- Length
- 179 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein rhoa
- EC
- 3.6.5.2
- UniProt
- P61586
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming protein rhoa (EC 3.6.5.2) | protein | 179 | 37% helix, 23% strand | P61586 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- DIO · 1,4-diethylene dioxide · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.51 | 0.77 | 38 | GDP, MG, DIO |
| 2 | 54 | 0.32 | 0.77 | 10 | 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 P61586
- Elsewhere: RCSB PDB 6V6U · PDBe 6V6U · UniProt P61586
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