Current Protein Identity:Q14674 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
7NJ0 CryoEM structure of the human Separase-Cdk1-cyclin B1-Cks1 complex Deposited 2021-02-14 Assembly 1 Insufficient information Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–2120(2120 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7NJ1 CryoEM structure of the human Separase-Securin complex Deposited 2021-02-14 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–2120(2120 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
9HM7 Cryo-EM structure of apo human separase with the mutation C2029S Deposited 2024-12-06 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–2120(2120 aa)
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9HMA Cryo-EM structure of apo human separase Deposited 2024-12-07 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–2120(2120 aa)
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9HMS Cryo-EM structure of human separase bound to SCC1 (310-550 aa) and SA2 Deposited 2024-12-09 Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain C 1–1481(1481 aa)
Chain C 1537–2120(584 aa)
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9HN0 Cryo-EM structure of human separase bound to SCC1 (310-550 aa) Deposited 2024-12-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–1481(1481 aa)
Chain B 1537–2120(584 aa)
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9HN4 Cryo-EM structure of human separase bound to phosphorylated SCC1 (310-550 aa) Deposited 2024-12-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 1–1481(1481 aa)
Chain B 1537–2120(584 aa)
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.93 Å
9HN5 Cryo-EM structure of human separase bound to phosphorylated SCC1 (100-320 aa) Deposited 2024-12-10 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–1481(1481 aa)
Chain A 1537–2120(584 aa)
Mutation:C2029S Mutation:C2029S ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.96 Å
9HVY Cryo-EM structure of human separase-SCC1 (1-631) fusion protein Deposited 2025-01-02 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–2120(2120 aa)
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å