8rl6

DNA helicase RECQL5 in complex with homo Di-Gluebody G5-006 - RECQL5 local refinement

Method: ELECTRON MICROSCOPY Dmax: 80.9 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 12–453 Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.18 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 1
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 8rl6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rl6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rl6
Deposition date deposition_date2024-01-02
Structure title titleDNA helicase RECQL5 in complex with homo Di-Gluebody G5-006 - 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_guinier25.32
Radius of gyration Rg (electron density) rg_electron24.39
Forward intensity I(0) i036122100.00
Molecular weight molecular_weight46647.0 kDa
Excluded volume excluded_volume58545 ų
Envelope volume envelope_volume70212 ų
Hydration-shell volume shell_volume24267 ų
Envelope diameter envelope_diameter84.6
Shell Rg shell_rg31.35
Envelope Rg envelope_rg24.31
Shape Rg shape_rg24.38
Total Rg total_rg25.25
Total atoms total_atoms6493
Residues n_residues436
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 dmax80.9
Rg (real space) rg_real25.34
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real3.6120e+07
I(0) uncertainty (real space) i0_real_error5.2040e+05
Rg (reciprocal space) rg_reciprocal25.33
I(0) (reciprocal space) i0_reciprocal36120000.0000
Solution quality estimate total_estimate0.9006
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.328
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5651000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)