7zmo

Crystal structure of human RECQL5 helicase APO form in complex with engineered nanobody (Gluebody) G3-052

Method: X-RAY DIFFRACTION Dmax: 153.3 Å Quality: GOOD

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 11–453 Not recorded Gluebody G3-052 × 1 ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1M ammonium sulfate -- 0.5% PEG8000 -- 0.1M HEPES pH 7.0 Resolution 3.75 Å R-free 0.306
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 11–453 Not recorded Gluebody G3-052 × 1 ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1M ammonium sulfate -- 0.5% PEG8000 -- 0.1M HEPES pH 7.0 Resolution 3.75 Å R-free 0.306

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 50 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 3–445; UniProt 11–453 Author chain B; PDBConstruct 3–445; UniProt 11–453

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 7zmo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7zmo
Deposition date deposition_date2022-04-19
Structure title titleCrystal structure of human RECQL5 helicase APO form in complex with engineered nanobody (Gluebody) G3-052
Keywords keywordsHelicase, Apo form, Nanobody complex, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.23
Radius of gyration Rg (electron density) rg_electron45.61
Forward intensity I(0) i0232797000.00
Molecular weight molecular_weight122030.0 kDa
Excluded volume excluded_volume151330 ų
Envelope volume envelope_volume223940 ų
Hydration-shell volume shell_volume42870 ų
Envelope diameter envelope_diameter156.0
Shell Rg shell_rg47.99
Envelope Rg envelope_rg43.72
Shape Rg shape_rg45.59
Total Rg total_rg45.79
Total atoms total_atoms8560
Residues n_residues1130
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 dmax153.3
Rg (real space) rg_real45.49
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real2.3280e+08
I(0) uncertainty (real space) i0_real_error4.9530e+06
Rg (reciprocal space) rg_reciprocal45.23
I(0) (reciprocal space) i0_reciprocal232700000.0000
Solution quality estimate total_estimate0.8529
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.328
Kurtosis Kurtosis kurtosis-0.695
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10730000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.735; Smooth: 0.787

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7zmoA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id7zmoA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id7zmoB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id7zmoB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id7zmoC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7zmoK01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)