9hms

Cryo-EM structure of human separase bound to SCC1 (310-550 aa) and SA2

Method: ELECTRON MICROSCOPY Dmax: 217.7 Å Quality: GOOD

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

Cohesin subunit SA-2

Homo sapiens

UniProt Q8N3U4

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1231 Not recorded Double-strand-break repair protein rad21 homolog × 1 (O60216) Separin × 1 (Q14674) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STAG2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1231; UniProt 1–1231

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 310–550 Not recorded Cohesin subunit SA-2 × 1 (Q8N3U4) Separin × 1 (Q14674) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–241; UniProt 310–550

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–1481 Chain C; UniProt 1537–2120 Not recorded Cohesin subunit SA-2 × 1 (Q8N3U4) 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 3.40 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 3
Chains and sequence ranges Author chain C; PDBConstruct 56–1536; UniProt 1–1481 Author chain C; 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 9hms

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9hms
Deposition date deposition_date2024-12-09
Structure title titleCryo-EM structure of human separase bound to SCC1 (310-550 aa) and SA2
Keywords keywordsSeparase, cell cycle, SCC1, RAD21, protease, chromosome segregation, Auto-cleavage, SA1/2, cohesin; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.46
Radius of gyration Rg (electron density) rg_electron60.84
Forward intensity I(0) i0805633000.00
Molecular weight molecular_weight240400.0 kDa
Excluded volume excluded_volume302290 ų
Envelope volume envelope_volume471910 ų
Hydration-shell volume shell_volume68342 ų
Envelope diameter envelope_diameter219.6
Shell Rg shell_rg56.45
Envelope Rg envelope_rg59.45
Shape Rg shape_rg60.83
Total Rg total_rg60.75
Total atoms total_atoms16909
Residues n_residues2181
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 dmax217.7
Rg (real space) rg_real61.02
Rg uncertainty (real space) rg_real_error3.24
I(0) (real space) i0_real8.0560e+08
I(0) uncertainty (real space) i0_real_error1.7470e+07
Rg (reciprocal space) rg_reciprocal59.93
I(0) (reciprocal space) i0_reciprocal804200000.0000
Solution quality estimate total_estimate0.7581
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.392
Kurtosis Kurtosis kurtosis-0.662
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41830000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.676; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.823; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)