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Crystal structure of human ankyrin G death domain
Analyse Crystal structure of human ankyrin G death domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O6X
- Type
- protein
- Length
- 193 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ankyrin-3
- UniProt
- Q12955
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ankyrin-3 | protein | 98 | 78% helix, 2% strand | Q12955 |
| B | Ankyrin-3 | protein | 95 | 76% helix, 0% strand | Q12955 |
Interfaces
1 interface between chains.
- A–B · 657 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 4O6X · Crystal structure of human Ankyrin G death domain · 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 Q12955
- Elsewhere: RCSB PDB 4O6X · PDBe 4O6X · UniProt Q12955
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