8p0a

Human Cohesin ATPase module

Method: ELECTRON MICROSCOPY Dmax: 92.2 Å Quality: GOOD

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

Structural maintenance of chromosomes protein 1A

Homo sapiens

UniProt Q14683

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 1–200 Chain A; UniProt 992–1233 Not recorded Structural maintenance of chromosomes protein 3 × 1 (Q9UQE7) 64-kDa C-terminal product × 1 (O60216) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.2 cryo-EM buffer:pH 8.2 cryo-EM buffer:pH 8.2 cryo-EM vitrification conditions:Cryogen ETHANE cryo-EM vitrification conditions:Cryogen ETHANE cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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.

12 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMC1A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–200; UniProt 1–200 Author chain A; PDBConstruct 215–456; UniProt 992–1233

Structural maintenance of chromosomes protein 3

Homo sapiens

UniProt Q9UQE7

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 1–211 Chain B; UniProt 979–1217 Not recorded Structural maintenance of chromosomes protein 1A × 1 (Q14683) 64-kDa C-terminal product × 1 (O60216) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.2 cryo-EM buffer:pH 8.2 cryo-EM buffer:pH 8.2 cryo-EM vitrification conditions:Cryogen ETHANE cryo-EM vitrification conditions:Cryogen ETHANE cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMC3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–211; UniProt 1–211 Author chain B; PDBConstruct 224–462; UniProt 979–1217

64-kDa C-terminal product

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 C; UniProt 558–629 Not recorded Structural maintenance of chromosomes protein 1A × 1 (Q14683) Structural maintenance of chromosomes protein 3 × 1 (Q9UQE7) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.2 cryo-EM buffer:pH 8.2 cryo-EM buffer:pH 8.2 cryo-EM vitrification conditions:Cryogen ETHANE cryo-EM vitrification conditions:Cryogen ETHANE cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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 3
Chains and sequence ranges Author chain C; PDBConstruct 2–73; UniProt 558–629

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 8p0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p0a
Deposition date deposition_date2023-05-10
Structure title titleHuman Cohesin ATPase module
Keywords keywords3D genome organization, Chromatin, Cohesin, ATPase activity, ATPase cycle, Cell cycle, DNA binding, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.17
Radius of gyration Rg (electron density) rg_electron27.32
Forward intensity I(0) i0105875000.00
Molecular weight molecular_weight81842.0 kDa
Excluded volume excluded_volume102860 ų
Envelope volume envelope_volume125830 ų
Hydration-shell volume shell_volume37417 ų
Envelope diameter envelope_diameter98.6
Shell Rg shell_rg35.49
Envelope Rg envelope_rg27.55
Shape Rg shape_rg27.30
Total Rg total_rg28.18
Total atoms total_atoms5755
Residues n_residues718
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 dmax92.2
Rg (real space) rg_real28.04
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.0590e+08
I(0) uncertainty (real space) i0_real_error1.4610e+06
Rg (reciprocal space) rg_reciprocal28.08
I(0) (reciprocal space) i0_reciprocal105900000.0000
Solution quality estimate total_estimate0.8857
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.6
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.381
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23780000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.910

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)