Research workbench
Crystal structure of the dimerization domain of doublesex protein from D. melanogaster
Analyse Crystal structure of the dimerization domain of doublesex protein from D.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZV1
- Type
- protein
- Length
- 118 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Doublesex protein
- UniProt
- P23023
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Doublesex protein | protein | 59 | 78% helix, 0% strand | P23023 |
Interfaces
1 interface between chains.
- A–B · 1203 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1ZV1 · Crystal structure of the dimerization domain of doublesex protein from D. melanogaster · the same entry in another collection · chain A against A, TM-score 1.00
- P23023 · AlphaFold monomer V2.0 prediction for protein doublesex (P23023) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P23023
- Elsewhere: RCSB PDB 1ZV1 · PDBe 1ZV1 · UniProt P23023
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