Research workbench
Cryoem structure of the human separase-CDK1-cyclin B1-CKS1 complex
Analyse Cryoem structure of the human separase-CDK1-cyclin B1-CKS1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NJ0
- Type
- protein
- Length
- 1,818 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O95997, Q14674, P06493, P14635, P61024
- Ligands
- PO4
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1188 | — | O95997, Q14674 |
| B | — | protein | 290 | — | P06493 |
| C | — | protein | 270 | — | P14635 |
| D | — | protein | 70 | — | P61024 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NJ0 · CryoEM structure of the human Separase-Cdk1-cyclin B1-Cks1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P14635 · AlphaFold monomer V2.0 prediction for G2/MITOTIC-specific cyclin-B1 (P14635) · a predicted model of the same protein · chain C against A, TM-score 0.99
- Q14674 · AlphaFold monomer V2.0 prediction for separin (Q14674) · a predicted model of the same protein · chain A against A, TM-score 0.95
- P61024 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinases regulatory subunit 1… · a predicted model of the same protein · chain D against A, TM-score 0.94
- P06493 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 1 (P06493) · a predicted model of the same protein · chain B against A, TM-score 0.91
- O95997 · AlphaFold monomer V2.0 prediction for securin (O95997) · a predicted model of the same protein · chain A against A, TM-score 0.07
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 O95997
- Every structure of UniProt Q14674
- Every structure of UniProt P06493
- Every structure of UniProt P14635
- Every structure of UniProt P61024
- Elsewhere: RCSB PDB 7NJ0 · PDBe 7NJ0 · UniProt O95997 · UniProt Q14674 · UniProt P06493 · UniProt P14635 · UniProt P61024
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