Research workbench
Structure of apo KANK1 ankyrin domain
Analyse Structure of apo KANK1 ankyrin domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YBJ
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kn motif and ankyrin repeat domain-containing protein 1
- UniProt
- Q14678
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kn motif and ankyrin repeat domain-containing protein 1 | protein | 248 | 57% helix, 0% strand | Q14678 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q14678
- Elsewhere: RCSB PDB 5YBJ · PDBe 5YBJ · UniProt Q14678
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