Research workbench
Structure of the thermotoga maritima HK853-BEF3-RR468 complex at pH 5.0
Analyse Structure of the thermotoga maritima HK853-BEF3-RR468 complex at pH 5.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UHT
- Type
- protein
- Length
- 716 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor histidine kinase; Response regulator
- UniProt
- Q9WZV7, Q9WYT9
- Ligands
- ADP, MG, SO4
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Sensor histidine kinase | protein | 237 | 50% helix, 21% strand | Q9WZV7 |
| B, D | Response regulator | protein | 121 | 40% helix, 19% strand | Q9WYT9 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, C
- MG · Magnesium ion · metal · 2 copies · chains B, D
- SO4 · Sulfate ion · ion · 3 copies · chains A, D, B
- GOL · Glycerol · additive · 9 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1089 | 0.83 | 0.84 | 112 | GOL, ADP, SO4 |
| 2 | 837 | 0.82 | 0.85 | 84 | ADP, SO4 |
| 3 | 85 | 0.43 | 0.80 | 16 | empty |
Interfaces
5 interfaces between chains.
- A–C · 1723 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 837 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 836 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 207 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 137 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 5UHT · Structure of the Thermotoga maritima HK853-BeF3-RR468 complex at pH 5.0 · 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 Q9WZV7
- Every structure of UniProt Q9WYT9
- Elsewhere: RCSB PDB 5UHT · PDBe 5UHT · UniProt Q9WZV7 · UniProt Q9WYT9
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