Research workbench
Crystal structure of the P93A monomer mutant of S. cerevisiae CKS1
Analyse Crystal structure of the P93A monomer mutant of S. cerevisiae CKS1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QY2
- Type
- protein
- Length
- 210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin-dependent kinases regulatory subunit
- UniProt
- P20486
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin-dependent kinases regulatory subunit | protein | 105 | 25% helix, 22% strand | P20486 |
| B | Cyclin-dependent kinases regulatory subunit | protein | 105 | 27% helix, 22% strand | P20486 |
Ligands and binding sites
- FLC · Citrate anion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 822 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3QY2 · Crystal structure of the P93A monomer mutant of S. cerevisiae Cks1 · the same entry in another collection · chain A against A, TM-score 1.00
- P20486 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinases regulatory subunit (P20486) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P20486
- Elsewhere: RCSB PDB 3QY2 · PDBe 3QY2 · UniProt P20486
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