Research workbench
H-RAS soaked in 90% R,S,R-bisfuranol: one of 10 in mscs set
Analyse H-RAS soaked in 90% R,S,R-bisfuranol: one of 10 in mscs set in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RSL
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase HRAS
- UniProt
- P01112
- Ligands
- RSF, GNP, CA, MG
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase HRAS | protein | 156 | 32% helix, 28% strand | P01112 |
Ligands and binding sites
- RSF · (3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-ol · ligand · 13 copies · chains A
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- MG · Magnesium ion · metal · 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 | 158 | 0.54 | 0.80 | 31 | GNP, RSF, MG |
Compared structures
- 3RSL · H-Ras soaked in 90% R,S,R-bisfuranol: one of 10 in MSCS set · the same entry in another collection · chain A against A, TM-score 1.00
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 P01112
- Elsewhere: RCSB PDB 3RSL · PDBe 3RSL · UniProt P01112
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