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Crystal structure of the kelch domain of human KLHL7
Analyse Crystal structure of the kelch domain of human KLHL7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3II7
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like protein 7
- UniProt
- Q8IXQ5
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like protein 7 | protein | 288 | 0% helix, 52% strand | Q8IXQ5 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 25 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 636 | 0.78 | 0.83 | 47 | EDO |
| 2 | 50 | 0.25 | 0.73 | 17 | empty |
Compared structures
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 Q8IXQ5
- Elsewhere: RCSB PDB 3II7 · PDBe 3II7 · UniProt Q8IXQ5
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