MolNFT v1 · #130041 · protein
Refined crystal structure of the triphosphate conformation of H-RAS P21 at 1.35 ångströms resolution: implications for the mechanism of GTP hydrolysis
5P21 · C-H-RAS P21 protein: “Refined crystal structure of the triphosphate conformation of H-RAS P21 at 1.35 ångströms resolution…”. X-ray diffraction, 2 ligands (GNP, MG), 1 pocket (best druggability 0.51). MolNFT v1 #130041 on GenesisL1…
- PDB
- 5P21
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-H-RAS P21 protein
- UniProt
- P01112
- Ligands
- GNP, MG
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-H-RAS P21 protein | protein | 166 | 36% helix, 27% strand | P01112 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · 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 | 219 | 0.51 | 0.76 | 31 | MG, GNP |
Compared structures
- 5P21 · Refined crystal structure of the triphosphate conformation of H-RAS P21 at 1.35 ångströms… · 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 5P21 · PDBe 5P21 · UniProt P01112
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