9hn5

Cryo-EM structure of human separase bound to phosphorylated SCC1 (100-320 aa)

Method: ELECTRON MICROSCOPY Dmax: 156.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Double-strand-break repair protein rad21 homolog

Homo sapiens

UniProt O60216

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 100–320 Non-standard monomer:Yes (specific site not provided by mmCIF) Separin × 1 (Q14674) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

35 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAD21_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–227; UniProt 100–320

Separin

Homo sapiens

UniProt Q14674

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–1481 Chain A; UniProt 1537–2120 Mutation:C2029S Double-strand-break repair protein rad21 homolog × 1 (O60216) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.96 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ESPL1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 56–1536; UniProt 1–1481 Author chain A; PDBConstruct 1549–2132; UniProt 1537–2120

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9hn5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9hn5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9hn5
Deposition date deposition_date2024-12-10
Structure title titleCryo-EM structure of human separase bound to phosphorylated SCC1 (100-320 aa)
Keywords keywordsSeparase, cell cycle, SCC1, RAD21, protease, chromosome segregation, Auto-cleavage, cohesin; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier44.52
Radius of gyration Rg (electron density) rg_electron44.05
Forward intensity I(0) i0385598000.00
Molecular weight molecular_weight160860.0 kDa
Excluded volume excluded_volume201580 ų
Envelope volume envelope_volume277800 ų
Hydration-shell volume shell_volume56319 ų
Envelope diameter envelope_diameter169.0
Shell Rg shell_rg44.59
Envelope Rg envelope_rg45.01
Shape Rg shape_rg44.18
Total Rg total_rg43.65
Total atoms total_atoms11314
Residues n_residues1516
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax156.7
Rg (real space) rg_real45.10
Rg uncertainty (real space) rg_real_error1.98
I(0) (real space) i0_real3.8560e+08
I(0) uncertainty (real space) i0_real_error7.7930e+06
Rg (reciprocal space) rg_reciprocal44.52
I(0) (reciprocal space) i0_reciprocal385300000.0000
Solution quality estimate total_estimate0.7751
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.3
Skewness Skewness skewness0.660
Kurtosis Kurtosis kurtosis-0.097
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57880000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.648; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.669; Smooth: 0.458

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)