Research workbench
Fitting results in the I-layer of the subnanometer structure of the bacterial PKM101 type IV secretion system core complex digested with elastase
Analyse Fitting results in the I-layer of the subnanometer structure of the bacterial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZBJ
- Type
- protein
- Length
- 1,568 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trao protein
- UniProt
- Q46704
- Pockets
- 14 · best druggability 0.70
Structure
electron microscopy · 1 distinct chain · 0% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | Trao protein | protein | 112 | 0% helix, 4% strand | Q46704 |
Pockets
14 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 346 | 0.70 | 0.82 | 50 | empty |
| 2 | 321 | 0.69 | 0.83 | 51 | empty |
| 3 | 320 | 0.69 | 0.83 | 51 | empty |
| 4 | 327 | 0.69 | 0.82 | 49 | empty |
| 5 | 289 | 0.69 | 0.83 | 49 | empty |
Interfaces
14 interfaces between chains.
- F–G · 851 Ų buried · 7 hydrogen bonds · protein-protein
- H–I · 851 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 849 Ų buried · 7 hydrogen bonds · protein-protein
- I–J · 848 Ų buried · 7 hydrogen bonds · protein-protein
- G–H · 848 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3ZBJ · Fitting results in the I-layer of the subnanometer structure of the bacterial pKM101 type… · 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 Q46704
- Elsewhere: RCSB PDB 3ZBJ · PDBe 3ZBJ · UniProt Q46704
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