Research workbench
The solution structure and dynamics of RAS P21. GDP determined by heteronuclear three and four dimensional NMR spectroscopy
Analyse The solution structure and dynamics of RAS P21. GDP determined by heteronuclear… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CRP
- 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
- 1 · best druggability 0.47
Structure
solution nmr · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-H-RAS P21 protein | protein | 166 | 33% helix, 19% strand | P01112 |
Ligands and binding sites
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 | 145 | 0.47 | 0.77 | 30 | MG, GDP |
Compared structures
- 1CRP · 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 1CRP · PDBe 1CRP · UniProt P01112
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