Research workbench
BTB domain of KLHL26
Analyse BTB domain of KLHL26 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 9ETW
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.51
- Source
- Homo sapiens
- Molecule
- Kelch-like protein 26
- UniProt
- Q53HC5
Structure
x-ray diffraction · resolution 1.51 · 1 distinct chain · 56% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Kelch-like protein 26 | protein | 125 | 56% helix, 17% strand | Q53HC5 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 2027 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- Q53HC5 · AlphaFold monomer V2.0 prediction for kelch-like protein 26 (Q53HC5) · 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 Q53HC5
- Elsewhere: RCSB PDB 9ETW · PDBe 9ETW · UniProt Q53HC5
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