MolNFT v1 · #37791 · protein
Crystal structure of the human rhoc-GDP complex
2GCN · Rho-related GTP-binding protein rhoc: “Crystal structure of the human rhoc-GDP complex”. X-ray diffraction, 2 ligands (GDP, MG), 2 pockets (best druggability 0.41). MolNFT v1 #37791 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2GCN
- Type
- protein
- Length
- 177 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
- GDP, MG
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho-related GTP-binding protein rhoc | protein | 177 | 38% helix, 23% strand | P08134 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
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 | 106 | 0.41 | 0.77 | 24 | MG, GDP |
| 2 | 51 | 0.29 | 0.75 | 15 | empty |
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 2GCN · PDBe 2GCN · UniProt P08134
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