Research workbench
Crystal structure of the receiver domain of a. thaliana cytokinin receptor ATCRE1 in complex with K+
Analyse Crystal structure of the receiver domain of a. thaliana cytokinin receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P8C
- Type
- protein
- Length
- 253 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receiver domain of histidine kinase 4
- EC
- 2.7.13.3, 3.1.3.16
- UniProt
- Q9C5U0
- Ligands
- K
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receiver domain of histidine kinase 4 (EC 2.7.13.3, 3.1.3.16) | protein | 133 | 42% helix, 17% strand | Q9C5U0 |
| B | Receiver domain of histidine kinase 4 (EC 2.7.13.3, 3.1.3.16) | protein | 120 | 44% helix, 18% strand | Q9C5U0 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.48 | 0.86 | 18 | empty |
| 2 | 51 | 0.25 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1583 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 7P8C · Crystal structure of the Receiver domain of A. thaliana cytokinin receptor AtCRE1 in… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9C5U0 · AlphaFold monomer V2.0 prediction for histidine kinase 4 (Q9C5U0) · a predicted model of the same protein · chain B against A, TM-score 0.79
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 Q9C5U0
- Elsewhere: RCSB PDB 7P8C · PDBe 7P8C · UniProt Q9C5U0
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