Research workbench
Crystal structure of the fusion protein linked by rhoa and the gap domain of mgcracgap
Analyse Crystal structure of the fusion protein linked by rhoa and the gap domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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