Research workbench
X-ray structure of cytokinin OXIDASE/DEHYDROGENASE (ckx) from arabidopsis thaliana AT5G21482
Analyse X-ray structure of cytokinin OXIDASE/DEHYDROGENASE (ckx) from arabidopsis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EXR
- Type
- protein
- Length
- 491 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytokinin dehydrogenase 7
- EC
- 1.5.99.12
- UniProt
- Q9FUJ1
- Ligands
- FAD
- Pockets
- 6 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytokinin dehydrogenase 7 (EC 1.5.99.12) | protein | 491 | 33% helix, 23% strand | Q9FUJ1 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1073 | 0.87 | 0.88 | 116 | FAD |
| 2 | 115 | 0.47 | 0.80 | 21 | empty |
| 3 | 91 | 0.39 | 0.77 | 30 | empty |
| 4 | 84 | 0.32 | 0.74 | 21 | empty |
| 5 | 69 | 0.29 | 0.73 | 15 | empty |
Modifications
Observed in the structure: 8 modified, 1 cofactor (engineered, flavinylation).
Compared structures
- 2EXR · X-Ray Structure of Cytokinin Oxidase/Dehydrogenase (CKX) From Arabidopsis Thaliana… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9FUJ1 · AlphaFold monomer V2.0 prediction for cytokinin dehydrogenase 7 (Q9FUJ1) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9FUJ1
- Elsewhere: RCSB PDB 2EXR · PDBe 2EXR · UniProt Q9FUJ1
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