MolNFT v1 · #114665 · protein
Structural characterization and modeling of the borrelia burgdorferi hybrid histidine kinase HK1 periplasmic sensor
5BWJ · Sensory transduction histidine kinase, putative: “Structural characterization and modeling of the borrelia burgdorferi hybrid histidine kinase HK1 periplasmic…”. X-ray diffraction, 2 ligands (MG, NO3), 12 pockets (best druggability…
- PDB
- 5BWJ
- Type
- protein
- Length
- 796 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensory transduction histidine kinase, putative
- UniProt
- O51381
- Ligands
- MG, NO3
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 27% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensory transduction histidine kinase, putative | protein | 195 | 27% helix, 36% strand | O51381 |
| B | Sensory transduction histidine kinase, putative | protein | 196 | 26% helix, 35% strand | O51381 |
| C | Sensory transduction histidine kinase, putative | protein | 202 | 26% helix, 35% strand | O51381 |
| D | Sensory transduction histidine kinase, putative | protein | 203 | 27% helix, 33% strand | O51381 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.77 | 0.97 | 28 | empty |
| 2 | 111 | 0.76 | 0.96 | 29 | empty |
| 3 | 103 | 0.75 | 0.96 | 29 | empty |
| 4 | 109 | 0.74 | 0.94 | 32 | empty |
| 5 | 148 | 0.67 | 0.88 | 33 | empty |
Interfaces
4 interfaces between chains.
- C–D · 1640 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1623 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 297 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 33 Ų buried · 0 hydrogen bonds · protein-protein
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 O51381
- Elsewhere: RCSB PDB 5BWJ · PDBe 5BWJ · UniProt O51381
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