MolNFT v1 · #159769 · protein
Crystal structure of GDP-bound human rala in a covalent complex with aryl sulfonyl fluoride compounds.
6P0K · RAS-related protein ral-a: “Crystal structure of GDP-bound human rala in a covalent complex with aryl sulfonyl fluoride compounds.”. X-ray diffraction, 4 ligands (NLV, GDP, CA), 2 pockets (best druggability 0.45). MolNFT v1 #159769…
- PDB
- 6P0K
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAS-related protein ral-a
- UniProt
- P11233
- Ligands
- NLV, GDP, CA, CL
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | RAS-related protein ral-a | protein | 168 | 40% helix, 26% strand | P11233 |
Ligands and binding sites
- NLV · 4-[(6-chloropyridin-2-yl)sulfamoyl]benzene-1-sulfonic acid · ligand · chains B
- GDP · Guanosine-5'-diphosphate · ligand · chains B
- CA · Calcium ion · metal · chains B
- CL · Chloride ion · ion · chains B
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 | 108 | 0.45 | 0.78 | 18 | NLV |
| 2 | 125 | 0.42 | 0.76 | 25 | CA, GDP |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6P0K · Crystal structure of GDP-bound human RalA in a covalent complex with aryl sulfonyl… · the same entry in another collection · chain B against B, TM-score 1.00
- P11233 · AlphaFold monomer V2.0 prediction for RAS-related protein ral-a (P11233) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P11233
- Elsewhere: RCSB PDB 6P0K · PDBe 6P0K · UniProt P11233
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.