MolNFT v1 · #3425 · protein
The solution structure and dynamics of RAS P21. GDP determined by heteronuclear three and four dimensional NMR spectroscopy
1CRQ · C-H-RAS P21 protein: “The solution structure and dynamics of RAS P21. GDP determined by heteronuclear three and four dimensional…”. Solution nmr, 2 ligands (GDP, MG), 2 pockets (best druggability 0.49). MolNFT v1 #3425 on GenesisL1…
- PDB
- 1CRQ
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-H-RAS P21 protein
- UniProt
- P01112
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.49
Structure
solution nmr · 1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-H-RAS P21 protein | protein | 166 | 36% helix, 24% strand | P01112 |
Ligands and binding sites
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 | 165 | 0.49 | 0.77 | 36 | MG, GDP |
| 2 | 50 | 0.32 | 0.77 | 15 | empty |
Compared structures
- 1CRQ · The solution structure and dynamics of RAS P21. GDP determined by heteronuclear three and… · 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 1CRQ · PDBe 1CRQ · UniProt P01112
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