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Crystal structure of the dimerization domain of zen-4
Analyse Crystal structure of the dimerization domain of zen-4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EQB
- Type
- protein
- Length
- 136 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin-like protein
- UniProt
- G5EG83
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 94% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin-like protein | protein | 68 | 91% helix, 0% strand | G5EG83 |
| B | Kinesin-like protein | protein | 68 | 97% helix, 0% strand | G5EG83 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1941 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 7EQB · Crystal structure of the dimerization domain of ZEN-4 · the same entry in another collection · chain A against A, TM-score 1.00
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 G5EG83
- Elsewhere: RCSB PDB 7EQB · PDBe 7EQB · UniProt G5EG83
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