Research workbench
Mouse rig-I ATPase domain
Analyse Mouse rig-I ATPase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TBK
- Type
- protein
- Length
- 524 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rig-I helicase domain
- EC
- 3.6.4.13
- UniProt
- Q6Q899
- Ligands
- ANP
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rig-I helicase domain (EC 3.6.4.13) | protein | 524 | 54% helix, 11% strand | Q6Q899 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 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 | 0.67 | 0.76 | 52 | empty |
| 2 | 76 | 0.46 | 0.82 | 22 | empty |
| 3 | 84 | 0.43 | 0.80 | 23 | empty |
| 4 | 145 | 0.42 | 0.75 | 24 | EDO |
| 5 | 73 | 0.33 | 0.75 | 21 | empty |
Modifications
Observed in the structure: 10 modified (engineered).
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 Q6Q899
- Elsewhere: RCSB PDB 3TBK · PDBe 3TBK · UniProt Q6Q899
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