Research workbench
CBDP35 semet structure
Analyse CBDP35 semet structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6S3Y
- Type
- protein
- Length
- 1,665 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PLYP35
- UniProt
- A8ATR6
- Pockets
- 12 · best druggability 0.59
Structure
x-ray diffraction · 5 distinct chains · 5% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, F, G, H, L, K | PLYP35 | protein | 139 | 4% helix, 54% strand | A8ATR6 |
| B | PLYP35 | protein | 140 | 6% helix, 56% strand | A8ATR6 |
| C | PLYP35 | protein | 139 | 6% helix, 56% strand | A8ATR6 |
| E, I | PLYP35 | protein | 138 | 4% helix, 56% strand | A8ATR6 |
| J | PLYP35 | protein | 137 | 4% helix, 55% strand | A8ATR6 |
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.59 | 0.79 | 34 | empty |
| 2 | 244 | 0.57 | 0.78 | 31 | empty |
| 3 | 241 | 0.56 | 0.78 | 30 | empty |
| 4 | 218 | 0.56 | 0.79 | 31 | empty |
| 5 | 260 | 0.56 | 0.77 | 33 | empty |
Interfaces
12 interfaces between chains.
- A–H · 937 Ų buried · 5 hydrogen bonds · protein-protein
- C–J · 935 Ų buried · 6 hydrogen bonds · protein-protein
- B–K · 927 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 906 Ų buried · 3 hydrogen bonds · protein-protein
- F–G · 544 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 45 modified (engineered).
Compared structures
- 6S3Y · CBDP35 SeMet structure · 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 A8ATR6
- Elsewhere: RCSB PDB 6S3Y · PDBe 6S3Y · UniProt A8ATR6
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