8rl9

RECQL5:sfGFP hetero dimer assembled by Di-Gluebody

Method: ELECTRON MICROSCOPY Dmax: 116.6 Å Quality: GOOD

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

Green fluorescent protein

Aequorea victoria

UniProt A0A059PIQ0

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–238 Not recorded Gluebody GbEnhancer × 1 Gluebody G5-006 × 1 ATP-dependent DNA helicase Q5 × 1 (O94762) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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.

91 other PDB entries and 137 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A059PIQ0_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–238; UniProt 1–238

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 12–453 Not recorded Green fluorescent protein × 1 (A0A059PIQ0) Gluebody GbEnhancer × 1 Gluebody G5-006 × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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 4
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 8rl9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rl9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rl9
Deposition date deposition_date2024-01-02
Structure title titleRECQL5:sfGFP hetero dimer assembled by Di-Gluebody
Keywords keywordsDNA helicase, Di-Gluebody, GFP, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.79
Radius of gyration Rg (electron density) rg_electron34.19
Forward intensity I(0) i0149417000.00
Molecular weight molecular_weight96135.0 kDa
Excluded volume excluded_volume119520 ų
Envelope volume envelope_volume157730 ų
Hydration-shell volume shell_volume39290 ų
Envelope diameter envelope_diameter115.0
Shell Rg shell_rg39.75
Envelope Rg envelope_rg33.74
Shape Rg shape_rg34.18
Total Rg total_rg34.67
Total atoms total_atoms13186
Residues n_residues894
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 dmax116.6
Rg (real space) rg_real34.85
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real1.4940e+08
I(0) uncertainty (real space) i0_real_error2.7440e+06
Rg (reciprocal space) rg_reciprocal34.82
I(0) (reciprocal space) i0_reciprocal149400000.0000
Solution quality estimate total_estimate0.8918
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.9
Skewness Skewness skewness0.343
Kurtosis Kurtosis kurtosis-0.467
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17980000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.938

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)