8rog

Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ATPgS-Mg-bound conformation

Method: X-RAY DIFFRACTION Dmax: 100.0 Å Quality: REASONABLE

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–175 Chain A; UniProt 1057–1233 Mutation:E1157Q 64-kDa C-terminal product × 1 (O60216) MG MAGNESIUM ION × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M sodium formate; 0.1 M Bis Tris propane pH 6.5; 20 % w/v PEG 3350 Resolution 1.94 Å R-free 0.253

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 1–175; UniProt 1–175 Author chain A; PDBConstruct 190–366; UniProt 1057–1233

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 558–629 Not recorded Structural maintenance of chromosomes protein 1A × 1 (Q14683) MG MAGNESIUM ION × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M sodium formate; 0.1 M Bis Tris propane pH 6.5; 20 % w/v PEG 3350 Resolution 1.94 Å R-free 0.253

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 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 8rog

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8rog
Deposition date deposition_date2024-01-11
Structure title titleHuman cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ATPgS-Mg-bound conformation
Keywords keywords3D genome organization, Chromatin, Cohesin, ATPase activity, ATPase cycle, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.37
Radius of gyration Rg (electron density) rg_electron24.39
Forward intensity I(0) i037083700.00
Molecular weight molecular_weight47029.0 kDa
Excluded volume excluded_volume58952 ų
Envelope volume envelope_volume72242 ų
Hydration-shell volume shell_volume25557 ų
Envelope diameter envelope_diameter101.3
Shell Rg shell_rg30.44
Envelope Rg envelope_rg25.11
Shape Rg shape_rg24.38
Total Rg total_rg25.13
Total atoms total_atoms3309
Residues n_residues419
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 dmax100.0
Rg (real space) rg_real25.45
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real3.7080e+07
I(0) uncertainty (real space) i0_real_error5.8250e+05
Rg (reciprocal space) rg_reciprocal25.42
I(0) (reciprocal space) i0_reciprocal37080000.0000
Solution quality estimate total_estimate0.6265
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks6
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.527
Kurtosis Kurtosis kurtosis0.200
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5962000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.253; Stabil: 0.919; Sysdev: 1.000; Positv: 1.000; Valcen: 0.623; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)