Research workbench
Structure of the pas domain from bordetella pertussis bvgs
Analyse Structure of the pas domain from bordetella pertussis bvgs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZJ8
- Type
- protein
- Length
- 1,028 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Virulence sensor protein bvgs
- EC
- 2.7.13.3
- UniProt
- P16575
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 8 distinct chains · 34% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Virulence sensor protein bvgs (EC 2.7.13.3) | protein | 141 | 37% helix, 30% strand | P16575 |
| B | Virulence sensor protein bvgs (EC 2.7.13.3) | protein | 133 | 38% helix, 30% strand | P16575 |
| C | Virulence sensor protein bvgs (EC 2.7.13.3) | protein | 119 | 35% helix, 34% strand | P16575 |
| D | Virulence sensor protein bvgs (EC 2.7.13.3) | protein | 115 | 34% helix, 36% strand | P16575 |
| E | Virulence sensor protein bvgs (EC 2.7.13.3) | protein | 133 | 35% helix, 32% strand | P16575 |
| F | Virulence sensor protein bvgs (EC 2.7.13.3) | protein | 138 | 34% helix, 30% strand | P16575 |
| G | Virulence sensor protein bvgs (EC 2.7.13.3) | protein | 136 | 32% helix, 31% strand | P16575 |
| H | Virulence sensor protein bvgs (EC 2.7.13.3) | protein | 113 | 26% helix, 33% strand | P16575 |
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 558 | 0.86 | 0.92 | 85 | empty |
| 2 | 565 | 0.86 | 0.92 | 81 | empty |
| 3 | 851 | 0.84 | 0.86 | 77 | empty |
| 4 | 358 | 0.84 | 0.92 | 40 | empty |
| 5 | 384 | 0.84 | 0.91 | 37 | empty |
Interfaces
16 interfaces between chains.
- A–C · 1818 Ų buried · 24 hydrogen bonds · protein-protein
- F–H · 1784 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 1776 Ų buried · 25 hydrogen bonds · protein-protein
- E–G · 1752 Ų buried · 22 hydrogen bonds · protein-protein
- E–H · 1104 Ų buried · 6 hydrogen bonds · 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 P16575
- Elsewhere: RCSB PDB 6ZJ8 · PDBe 6ZJ8 · UniProt P16575
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