MolNFT v1 · #114868 · protein
Crystal structure of the fusion protein linked by rhoa and the gap domain of mgcracgap
5C2K · Transforming protein RHOA,RAC GTPase-activating protein 1: “Crystal structure of the fusion protein linked by rhoa and the gap domain of mgcracgap”. X-ray diffraction, 3 ligands (AF3, GDP, MG), 2 pockets (best druggability 0.71).…
- PDB
- 5C2K
- Type
- protein
- Length
- 382 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein RHOA,RAC GTPase-activating protein 1
- UniProt
- P61586, Q9H0H5
- Ligands
- AF3, GDP, MG
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming protein RHOA,RAC GTPase-activating protein 1 | protein | 382 | 52% helix, 13% strand | P61586, Q9H0H5 |
Ligands and binding sites
- AF3 · Aluminum fluoride · ligand · chains A
- GDP · Guanosine-5'-diphosphate · 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 635 | 0.71 | 0.79 | 58 | MG, AF3, GDP |
| 2 | 149 | 0.48 | 0.77 | 31 | empty |
Compared structures
- 5C2K · Crystal structure of the fusion protein linked by RhoA and the GAP domain of MgcRacGAP · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H0H5 · AlphaFold monomer V2.0 prediction for rac GTPase-activating protein 1 (Q9H0H5) · a predicted model of the same protein · chain A against A, TM-score 0.52
- P61586 · AlphaFold monomer V2.0 prediction for transforming protein rhoa (P61586) · a predicted model of the same protein · chain A against A, TM-score 0.48
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 P61586
- Every structure of UniProt Q9H0H5
- Elsewhere: RCSB PDB 5C2K · PDBe 5C2K · UniProt P61586 · UniProt Q9H0H5
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