6wge

Cryo-EM structure of human Cohesin-NIPBL-DNA complex without STAG1

Method: ELECTRON MICROSCOPY Dmax: 174.9 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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–1233 Mutation:E1157Q Structural maintenance of chromosomes protein 3 × 1 (Q9UQE7) Double-strand-break repair protein rad21 homolog × 1 (O60216) Nipped-B-like protein × 1 (Q6KC79) DNA (43-MER) × 1 DNA (43-MER) × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–1233; UniProt 1–1233

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 1–1217 Mutation:E1144Q Structural maintenance of chromosomes protein 1A × 1 (Q14683) Double-strand-break repair protein rad21 homolog × 1 (O60216) Nipped-B-like protein × 1 (Q6KC79) DNA (43-MER) × 1 DNA (43-MER) × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–1217; UniProt 1–1217

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 1–631 Mutation:R172A, D279A, R450A Structural maintenance of chromosomes protein 1A × 1 (Q14683) Structural maintenance of chromosomes protein 3 × 1 (Q9UQE7) Nipped-B-like protein × 1 (Q6KC79) DNA (43-MER) × 1 DNA (43-MER) × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–631; UniProt 1–631

Nipped-B-like protein

Homo sapiens

UniProt Q6KC79

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain E; UniProt 1163–2804 Not recorded Structural maintenance of chromosomes protein 1A × 1 (Q14683) Structural maintenance of chromosomes protein 3 × 1 (Q9UQE7) Double-strand-break repair protein rad21 homolog × 1 (O60216) DNA (43-MER) × 1 DNA (43-MER) × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NIPBL_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–1642; UniProt 1163–2804

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 6wge

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wge
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wge
Deposition date deposition_date2020-04-05
Structure title titleCryo-EM structure of human Cohesin-NIPBL-DNA complex without STAG1
Keywords keywords;Protein-DNA complex, ATPase, DNA-binding protein, Genome organization, Sister chromatid cohesion, Transcription regulation, CELL CYCLE, CELL CYCLE-DNA complex ;; CELL CYCLE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.92
Radius of gyration Rg (electron density) rg_electron51.32
Forward intensity I(0) i01321360000.00
Molecular weight molecular_weight289220.0 kDa
Excluded volume excluded_volume356980 ų
Envelope volume envelope_volume547150 ų
Hydration-shell volume shell_volume90789 ų
Envelope diameter envelope_diameter178.2
Shell Rg shell_rg53.35
Envelope Rg envelope_rg50.50
Shape Rg shape_rg51.32
Total Rg total_rg51.41
Total atoms total_atoms20194
Residues n_residues2366
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 dmax174.9
Rg (real space) rg_real50.98
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real1.3210e+09
I(0) uncertainty (real space) i0_real_error2.2670e+07
Rg (reciprocal space) rg_reciprocal50.86
I(0) (reciprocal space) i0_reciprocal1321000000.0000
Solution quality estimate total_estimate0.8617
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.4
Skewness Skewness skewness0.410
Kurtosis Kurtosis kurtosis-0.287
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha193000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.769

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)