MolNFT v1 · #15497 · protein
Crystal structure of human RAB5A A30P mutant complex with GDP
1N6I · RAS-related protein rab-5A: “Crystal structure of human RAB5A A30P mutant complex with GDP”. X-ray diffraction, 2 ligands (GDP, MG), 1 pocket (best druggability 0.51). MolNFT v1 #15497 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1N6I
- Type
- protein
- Length
- 167 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related protein rab-5A
- UniProt
- P20339
- Ligands
- GDP, MG
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related protein rab-5A | protein | 167 | 39% helix, 29% strand | P20339 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.51 | 0.80 | 29 | MG, GDP |
Modifications
Observed in the structure: 1 covalent (additive adduct).
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 P20339
- Elsewhere: RCSB PDB 1N6I · PDBe 1N6I · UniProt P20339
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.