Research workbench
Crystal structure of the kelch domain of human KBTBD5
Analyse Crystal structure of the kelch domain of human KBTBD5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ASC
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch repeat and btb domain-containing protein 5
- UniProt
- Q2TBA0
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch repeat and btb domain-containing protein 5 | protein | 308 | 1% helix, 55% strand | Q2TBA0 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 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 | 762 | 0.78 | 0.82 | 67 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
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 Q2TBA0
- Elsewhere: RCSB PDB 4ASC · PDBe 4ASC · UniProt Q2TBA0
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