MolNFT v1 · #37793 · protein
Crystal structure of the human rhoc-gsp complex
2GCP · Rho-related GTP-binding protein rhoc: “Crystal structure of the human rhoc-gsp complex”. X-ray diffraction, 2 ligands (GSP, MG), 1 pocket (best druggability 0.56). MolNFT v1 #37793 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2GCP
- Type
- protein
- Length
- 178 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rho-related GTP-binding protein rhoc
- UniProt
- P08134
- Ligands
- GSP, MG
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho-related GTP-binding protein rhoc | protein | 178 | 39% helix, 25% strand | P08134 |
Ligands and binding sites
- GSP · 5'-guanosine-diphosphate-monothiophosphate · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · 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 | 151 | 0.56 | 0.82 | 34 | MG, GSP, EDO |
Compared structures
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 P08134
- Elsewhere: RCSB PDB 2GCP · PDBe 2GCP · UniProt P08134
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