MolNFT v1 · #57215 · protein
Catalytic domain of histidine kinase thka (TM1359) in complex with ADP and mg ion (trigonal)
3A0T · Sensor protein: “Catalytic domain of histidine kinase thka (TM1359) in complex with ADP and mg ion (trigonal)”. X-ray diffraction, 2 ligands (ADP, MG), 1 pocket (best druggability 0.64). MolNFT v1 #57215 on GenesisL1: 3D structure…
- PDB
- 3A0T
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein
- EC
- 2.7.13.3
- UniProt
- Q9X180
- Ligands
- ADP, MG
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein (EC 2.7.13.3) | protein | 152 | 36% helix, 31% strand | Q9X180 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 241 | 0.64 | 0.82 | 30 | MG, ADP |
Compared structures
- 3A0T · Catalytic domain of histidine kinase ThkA (TM1359) in complex with ADP and Mg ion… · 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 Q9X180
- Elsewhere: RCSB PDB 3A0T · PDBe 3A0T · UniProt Q9X180
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.