Research workbench
NMR structure of the cad domain of caspase-activated DNase
Analyse NMR structure of the cad domain of caspase-activated DNase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C9F
- Type
- protein
- Length
- 87 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-activated DNase
- UniProt
- O54788
Structure
solution nmr · 1 distinct chain · 13% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-activated DNase | protein | 87 | 13% helix, 25% strand | O54788 |
Compared structures
- 1C9F · NMR structure of the cad domain of caspase-activated DNase · the same entry in another collection · chain A against A, TM-score 1.00
- O54788 · AlphaFold monomer V2.0 prediction for DNA fragmentation factor subunit beta (O54788) · a predicted model of the same protein · chain A against A, TM-score 0.60
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 O54788
- Elsewhere: RCSB PDB 1C9F · PDBe 1C9F · UniProt O54788
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