Research workbench
Human trio residues 1284-1959 in complex with RAC1
Analyse Human trio residues 1284-1959 in complex with RAC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SJ4
- Type
- protein
- Length
- 481 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Triple functional domain protein; RAS-related C3 botulinum toxin substrate 1
- EC
- 2.7.11.1
- UniProt
- O75962, P63000
- Pockets
- 5 · best druggability 0.61
Structure
electron microscopy · 2 distinct chains · 51% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Triple functional domain protein (EC 2.7.11.1) | protein | 304 | 58% helix, 17% strand | O75962 |
| B | RAS-related C3 botulinum toxin substrate 1 | protein | 177 | 38% helix, 25% strand | P63000 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 268 | 0.61 | 0.80 | 34 | empty |
| 2 | 359 | 0.56 | 0.75 | 33 | empty |
| 3 | 222 | 0.52 | 0.76 | 30 | empty |
| 4 | 181 | 0.44 | 0.74 | 23 | empty |
| 5 | 66 | 0.31 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1367 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 7SJ4 · Human Trio residues 1284-1959 in complex with Rac1 · 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 O75962
- Every structure of UniProt P63000
- Elsewhere: RCSB PDB 7SJ4 · PDBe 7SJ4 · UniProt O75962 · UniProt P63000
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