Research workbench
Structure of yeast dcn-1
Analyse Structure of yeast dcn-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IS9
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Defective in cullin neddylation protein 1
- UniProt
- Q12395
- Ligands
- PT, CL
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Defective in cullin neddylation protein 1 | protein | 204 | 63% helix, 4% strand | Q12395 |
Ligands and binding sites
- PT · Platinum (II) ion · metal · chains A
- CL · Chloride ion · ion · 4 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q12395
- Elsewhere: RCSB PDB 2IS9 · PDBe 2IS9 · UniProt Q12395
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.