Research workbench
Crystal structure of a dual sensor histidine kinase in BEF3- bound state
Analyse Crystal structure of a dual sensor histidine kinase in BEF3- bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OAQ
- Type
- protein
- Length
- 603 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual sensor histidine kinase
- Ligands
- CYC, BEF, MG
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual sensor histidine kinase | protein | 302 | 44% helix, 21% strand | — |
| B | Dual sensor histidine kinase | protein | 301 | 47% helix, 23% strand | — |
Ligands and binding sites
- CYC · Phycocyanobilin · ligand · 2 copies · chains A, B
- BEF · Beryllium trifluoride ion · ligand · chains A
- MG · Magnesium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.76 | 0.87 | 31 | CYC |
| 2 | 280 | 0.74 | 0.87 | 32 | CYC |
| 3 | 411 | 0.70 | 0.82 | 56 | MG |
| 4 | 222 | 0.44 | 0.72 | 26 | empty |
| 5 | 63 | 0.44 | 0.82 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1891 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor, 2 disulfide (phycocyanobilin attachment, disulfide).
Compared structures
- 6OAQ · Crystal structure of a dual sensor histidine kinase in BeF3- bound state · 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
- Elsewhere: RCSB PDB 6OAQ · PDBe 6OAQ
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