Research workbench
Yeast betaprime cop 1-304 with ktktn motif
Analyse Yeast betaprime cop 1-304 with ktktn motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YNN
- Type
- protein
- Length
- 308 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coatomer subunit beta'; Ktktn motif
- UniProt
- P41811
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coatomer subunit beta' | protein | 300 | 3% helix, 55% strand | P41811 |
| P | Ktktn motif | protein | 8 | 0% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 668 | 0.80 | 0.85 | 54 | SO4 |
| 2 | 61 | 0.27 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–P · 355 Ų buried · 12 hydrogen bonds · protein-protein
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 P41811
- Elsewhere: RCSB PDB 2YNN · PDBe 2YNN · UniProt P41811
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