MolNFT v1 · #24608 · protein
Crystal structure of caspase-activated DNase (cad)
1V0D · DNA fragmentation factor 40 kda subunit: “Crystal structure of caspase-activated DNase (cad)”. X-ray diffraction, 3 ligands (ZN, MG, PB), 2 pockets (best druggability 0.44). MolNFT v1 #24608 on GenesisL1: 3D structure, binding sites…
- PDB
- 1V0D
- Type
- protein
- Length
- 244 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA fragmentation factor 40 kda subunit
- UniProt
- O54788
- Ligands
- ZN, MG, PB
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA fragmentation factor 40 kda subunit | protein | 244 | 47% helix, 7% strand | O54788 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- PB · Lead (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.44 | 0.78 | 19 | empty |
| 2 | 95 | 0.35 | 0.74 | 15 | MG |
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 O54788
- Elsewhere: RCSB PDB 1V0D · PDBe 1V0D · UniProt O54788
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