7zml

Crystal structure of human RECQL5 helicase APO form in complex with engineered nanobody (Gluebody) G1-001

Method: X-RAY DIFFRACTION Dmax: 149.8 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 G1-001 × 1 ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;293 K;0.1M bis-tris pH 5.9 -- 0.1M lithium sulfate -- 30% PEG3350 Resolution 2.79 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 11–453 Not recorded Gluebody G1-001 × 1 ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;293 K;0.1M bis-tris pH 5.9 -- 0.1M lithium sulfate -- 30% PEG3350 Resolution 2.79 Å R-free 0.261
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 11–453 Not recorded Gluebody G1-001 × 1 ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;293 K;0.1M bis-tris pH 5.9 -- 0.1M lithium sulfate -- 30% PEG3350 Resolution 2.79 Å R-free 0.261
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 11–453 Not recorded Gluebody G1-001 × 1 ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.9;293 K;0.1M bis-tris pH 5.9 -- 0.1M lithium sulfate -- 30% PEG3350 Resolution 2.79 Å R-free 0.261

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 48 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 Author chain C; PDBConstruct 3–445; UniProt 11–453 Author chain D; 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 7zml

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7zml
Deposition date deposition_date2022-04-19
Structure title titleCrystal structure of human RECQL5 helicase APO form in complex with engineered nanobody (Gluebody) G1-001
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_guinier46.85
Radius of gyration Rg (electron density) rg_electron46.85
Forward intensity I(0) i0947184000.00
Molecular weight molecular_weight251000.0 kDa
Excluded volume excluded_volume312930 ų
Envelope volume envelope_volume442790 ų
Hydration-shell volume shell_volume79716 ų
Envelope diameter envelope_diameter158.0
Shell Rg shell_rg50.62
Envelope Rg envelope_rg45.30
Shape Rg shape_rg46.81
Total Rg total_rg47.10
Total atoms total_atoms17607
Residues n_residues2283
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 dmax149.8
Rg (real space) rg_real46.74
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real9.4720e+08
I(0) uncertainty (real space) i0_real_error1.3070e+07
Rg (reciprocal space) rg_reciprocal46.85
I(0) (reciprocal space) i0_reciprocal947300000.0000
Solution quality estimate total_estimate0.8737
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.271
Kurtosis Kurtosis kurtosis-0.402
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47000000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.694

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id7zmlA01
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_id7zmlA02
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_id7zmlB01
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_id7zmlB02
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_id7zmlC01
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_id7zmlC02
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_id7zmlD01
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_id7zmlD02
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_id7zmlE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7zmlF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7zmlG01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7zmlK01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)