8rla

RECQL5:sfGFP hetero dimer assembled by Di-Gluebody - RECQL5 local refinement

Method: ELECTRON MICROSCOPY Dmax: 87.9 Å Quality: EXCELLENT

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

ATP-dependent DNA helicase Q5

Homo sapiens

UniProt O94762

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 12–453 Not recorded Gluebody G5-006 × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

28 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RECQ5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–442; UniProt 12–453

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 8rla

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rla
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8rla
Deposition date deposition_date2024-01-02
Structure title titleRECQL5:sfGFP hetero dimer assembled by Di-Gluebody - RECQL5 local refinement
Keywords keywordsDNA helicase, Di-Gluebody, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.62
Radius of gyration Rg (electron density) rg_electron27.85
Forward intensity I(0) i060695800.00
Molecular weight molecular_weight60007.0 kDa
Excluded volume excluded_volume74833 ų
Envelope volume envelope_volume94139 ų
Hydration-shell volume shell_volume29259 ų
Envelope diameter envelope_diameter95.5
Shell Rg shell_rg33.98
Envelope Rg envelope_rg27.81
Shape Rg shape_rg27.81
Total Rg total_rg28.62
Total atoms total_atoms8304
Residues n_residues560
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 dmax87.9
Rg (real space) rg_real28.58
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real6.0700e+07
I(0) uncertainty (real space) i0_real_error8.2950e+05
Rg (reciprocal space) rg_reciprocal28.60
I(0) (reciprocal space) i0_reciprocal60700000.0000
Solution quality estimate total_estimate0.9011
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary86.3
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9740000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.975; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.795

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)