Research workbench
Tetradecameric pilq bound by tsap heptamer from pseudomonas aeruginosa
Analyse Tetradecameric pilq bound by tsap heptamer from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VE2
- Type
- protein
- Length
- 6,153 residues
- Chains
- 21
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fimbrial assembly protein pilq; Lysm domain-containing protein
- UniProt
- P34750, Q9I7A7
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 2 distinct chains · 18% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | Fimbrial assembly protein pilq | protein | 327 | 20% helix, 55% strand | P34750 |
| O, P, Q, R, S, T, U | Lysm domain-containing protein | protein | 225 | 14% helix, 43% strand | Q9I7A7 |
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 | 1034 | 0.86 | 0.88 | 185 | empty |
| 2 | 1082 | 0.85 | 0.86 | 190 | empty |
| 3 | 822 | 0.83 | 0.86 | 127 | empty |
| 4 | 847 | 0.82 | 0.85 | 131 | empty |
| 5 | 697 | 0.82 | 0.86 | 123 | empty |
Interfaces
39 interfaces between chains.
- B–C · 1859 Ų buried · 35 hydrogen bonds · protein-protein
- D–E · 1852 Ų buried · 37 hydrogen bonds · protein-protein
- L–M · 1851 Ų buried · 36 hydrogen bonds · protein-protein
- F–G · 1849 Ų buried · 35 hydrogen bonds · protein-protein
- A–N · 1845 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 6VE2 · Tetradecameric PilQ bound by TsaP heptamer from Pseudomonas aeruginosa · the same entry in another collection · chain U against U, 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 P34750
- Every structure of UniProt Q9I7A7
- Elsewhere: RCSB PDB 6VE2 · PDBe 6VE2 · UniProt P34750 · UniProt Q9I7A7
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