Research workbench
Catalytic domain of histidine kinase thka (TM1359) for mad phasing (nucleotide free form 2, orthorombic)
Analyse Catalytic domain of histidine kinase thka (TM1359) for mad phasing (nucleotide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A0W
- Type
- protein
- Length
- 296 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein
- EC
- 2.7.13.3
- UniProt
- Q9X180
- Ligands
- EMC, EMT
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein (EC 2.7.13.3) | protein | 152 | 38% helix, 31% strand | Q9X180 |
| B | Sensor protein (EC 2.7.13.3) | protein | 144 | 38% helix, 33% strand | Q9X180 |
Ligands and binding sites
- EMC · Ethyl mercury ion · ligand · 4 copies · chains A, B
- EMT · 2-(ethylmercuri-thio)-benzoic acid · ligand · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A, B
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 | 487 | 0.67 | 0.78 | 47 | MPD |
| 2 | 185 | 0.54 | 0.78 | 25 | empty |
| 3 | 84 | 0.43 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 621 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3A0W · Catalytic domain of histidine kinase ThkA (TM1359) for MAD phasing (nucleotide free form… · the same entry in another collection · chain B against B, 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 Q9X180
- Elsewhere: RCSB PDB 3A0W · PDBe 3A0W · UniProt Q9X180
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.