7lto

Nse5-6 complex

Method: ELECTRON MICROSCOPY Dmax: 87.6 Å Quality: GOOD

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

Non-structural maintenance of chromosome element 5

Saccharomyces cerevisiae

UniProt Q03718

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–556 Not recorded Ubiquitin-like protein SMT3,DNA repair protein KRE29 chimera × 1 (Q12306,P40026) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 NSE5_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 12–567; UniProt 1–556

Ubiquitin-like protein SMT3,DNA repair protein KRE29 chimera

Saccharomyces cerevisiae

UniProt P40026

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–464 Not recorded Non-structural maintenance of chromosome element 5 × 1 (Q03718) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name KRE29_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 123–586; UniProt 1–464

Ubiquitin-like protein SMT3,DNA repair protein KRE29 chimera

Saccharomyces cerevisiae

UniProt Q12306

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–98 Not recorded Non-structural maintenance of chromosome element 5 × 1 (Q03718) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

95 other PDB entries and 116 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMT3_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 24–121; UniProt 1–98

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 7lto

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7lto
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7lto
Deposition date deposition_date2021-02-19
Structure title titleNse5-6 complex
Keywords keywordsSMC5/6, Nse5-6, Nse5, Nse6, complex, SUMO-binding, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.75
Radius of gyration Rg (electron density) rg_electron25.48
Forward intensity I(0) i065896100.00
Molecular weight molecular_weight67301.0 kDa
Excluded volume excluded_volume85832 ų
Envelope volume envelope_volume107130 ų
Hydration-shell volume shell_volume34146 ų
Envelope diameter envelope_diameter91.7
Shell Rg shell_rg33.71
Envelope Rg envelope_rg25.46
Shape Rg shape_rg25.49
Total Rg total_rg26.37
Total atoms total_atoms4754
Residues n_residues605
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 dmax87.6
Rg (real space) rg_real26.63
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real6.5900e+07
I(0) uncertainty (real space) i0_real_error7.3660e+05
Rg (reciprocal space) rg_reciprocal26.67
I(0) (reciprocal space) i0_reciprocal65900000.0000
Solution quality estimate total_estimate0.8892
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.6
Skewness Skewness skewness0.225
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19820000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)