MolNFT v1 · #18337 · protein
Crystallographic studies on P21H-RAS using synchrotron laue method: improvement of crystal quality and monitoring of the GTPase reaction at different time points
1PLK · C-H-RAS P21 protein: “Crystallographic studies on P21H-RAS using synchrotron laue method: improvement of crystal quality and…”. X-ray diffraction, 2 ligands (GTP, MG), 4 pockets (best druggability 0.73). MolNFT v1 #18337 on…
- PDB
- 1PLK
- Type
- protein
- Length
- 141 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-H-RAS P21 protein
- UniProt
- P01112
- Ligands
- GTP, MG
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-H-RAS P21 protein | protein | 141 | 26% helix, 11% strand | P01112 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 228 | 0.73 | 0.88 | 29 | empty |
| 2 | 160 | 0.59 | 0.83 | 31 | empty |
| 3 | 85 | 0.41 | 0.79 | 19 | empty |
| 4 | 124 | 0.40 | 0.75 | 28 | MG, GTP |
Compared structures
- 1PLK · Crystallographic studies on P21H-RAS using synchrotron laue method: improvement of… · 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 1PLK · PDBe 1PLK · UniProt P01112
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