MolNFT v1 · #15496 · protein
Crystal structure of human RAB5A
1N6H · RAS-related protein rab-5A: “Crystal structure of human RAB5A”. X-ray diffraction, 2 ligands (GNP, MG), 1 pocket (best druggability 0.49). MolNFT v1 #15496 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1N6H
- 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
- GNP, MG
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS-related protein rab-5A | protein | 167 | 38% helix, 29% strand | P20339 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.49 | 0.81 | 25 | MG, GNP |
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 1N6H · PDBe 1N6H · UniProt P20339
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