Research workbench
Cdtb double heptamer long form mask 1 modeled from cryo-EM MAP reconstructed using C7 symmetry
Analyse Cdtb double heptamer long form mask 1 modeled from cryo-EM MAP reconstructed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OKS
- Type
- protein
- Length
- 1,610 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosyltransferase binding component
- UniProt
- A8DS70
- Pockets
- 20 · best druggability 0.62
Structure
electron microscopy · 1 distinct chain · 4% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | ADP-ribosyltransferase binding component | protein | 115 | 4% helix, 42% strand | A8DS70 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.62 | 0.80 | 47 | empty |
| 2 | 258 | 0.61 | 0.79 | 46 | empty |
| 3 | 284 | 0.61 | 0.79 | 47 | empty |
| 4 | 271 | 0.60 | 0.79 | 48 | empty |
| 5 | 238 | 0.59 | 0.79 | 41 | empty |
Interfaces
21 interfaces between chains.
- A–J · 299 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 298 Ų buried · 2 hydrogen bonds · protein-protein
- B–K · 296 Ų buried · 0 hydrogen bonds · protein-protein
- A–G · 294 Ų buried · 2 hydrogen bonds · protein-protein
- G–I · 293 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6OKS · CDTb Double Heptamer Long Form Mask 1 Modeled from Cryo-EM Map Reconstructed using C7… · 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 A8DS70
- Elsewhere: RCSB PDB 6OKS · PDBe 6OKS · UniProt A8DS70
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