Research workbench
Crystal structure of the ATP-binding domain of desk in complex with ATP
Analyse Crystal structure of the ATP-binding domain of desk in complex with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EHG
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor kinase (yocf protein)
- EC
- 2.7.13.3
- UniProt
- O34757
- Ligands
- ATP, MG, IOD
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor kinase (yocf protein) (EC 2.7.13.3) | protein | 125 | 38% helix, 26% strand | O34757 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- IOD · Iodide ion · ion · 12 copies · chains A
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 | 120 | 0.55 | 0.83 | 22 | ATP, MG, IOD |
Compared structures
- 3EHG · Crystal structure of the ATP-binding domain of DesK in complex with ATP · the same entry in another collection · chain A against A, TM-score 1.00
- O34757 · AlphaFold monomer V2.0 prediction for sensor histidine kinase desk (O34757) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O34757
- Elsewhere: RCSB PDB 3EHG · PDBe 3EHG · UniProt O34757
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