MolNFT v1 · #144629 · protein
Structure of mouse rig-I tandem cards
6BZH · Probable ATP-dependent RNA helicase DDX58: “Structure of mouse rig-I tandem cards”. X-ray diffraction, 1 ligand (CL), 9 pockets (best druggability 0.87). MolNFT v1 #144629 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6BZH
- Type
- protein
- Length
- 954 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable ATP-dependent RNA helicase DDX58
- EC
- 3.6.4.13
- UniProt
- Q6Q899
- Ligands
- CL
- Pockets
- 9 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) | protein | 191 | 77% helix, 0% strand | Q6Q899 |
| B | Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) | protein | 192 | 75% helix, 0% strand | Q6Q899 |
| C | Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) | protein | 191 | 74% helix, 0% strand | Q6Q899 |
| D | Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) | protein | 189 | 73% helix, 0% strand | Q6Q899 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, B, D
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 549 | 0.87 | 0.93 | 76 | empty |
| 2 | 284 | 0.82 | 0.93 | 37 | empty |
| 3 | 221 | 0.78 | 0.92 | 40 | empty |
| 4 | 225 | 0.58 | 0.80 | 31 | empty |
| 5 | 94 | 0.45 | 0.80 | 26 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1009 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 999 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 993 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 988 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 327 Ų buried · 1 hydrogen bond · protein-protein
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 6BZH · PDBe 6BZH · UniProt Q6Q899
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