8bd4

TniQ-capped Tns-ATP-dsDNA complex

Method: ELECTRON MICROSCOPY Dmax: 131.3 Å Quality: GOOD

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

TnsC

Scytonema hofmannii

UniProt A0A8J0PCL3

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–276 Chain B; UniProt 1–276 Chain C; UniProt 1–276 Chain D; UniProt 1–276 Chain E; UniProt 1–276 Chain F; UniProt 1–276 Chain G; UniProt 1–276 Not recorded TniQ (Homology model) × 3 (A0A8J0PCL5) ;DNA (5'-D(P*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*C)-3') ; × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J0PCL3_9CYAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 1–276 Author chain B; PDBConstruct 1–276; UniProt 1–276 Author chain C; PDBConstruct 1–276; UniProt 1–276 Author chain D; PDBConstruct 1–276; UniProt 1–276 Author chain E; PDBConstruct 1–276; UniProt 1–276 Author chain F; PDBConstruct 1–276; UniProt 1–276 Author chain G; PDBConstruct 1–276; UniProt 1–276

TniQ (Homology model)

Scytonema hofmannii

UniProt A0A8J0PCL5

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain R; UniProt 1–167 Chain S; UniProt 1–167 Chain T; UniProt 1–167 Not recorded TnsC × 7 (A0A8J0PCL3) ;DNA (5'-D(P*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*C)-3') ; × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.44 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J0PCL5_9CYAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 1–167; UniProt 1–167 Author chain S; PDBConstruct 1–167; UniProt 1–167 Author chain T; PDBConstruct 1–167; UniProt 1–167

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 8bd4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bd4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bd4
Deposition date deposition_date2022-10-18
Structure title titleTniQ-capped Tns-ATP-dsDNA complex
Keywords keywordsTransposition, TniQ, TnsC, CRISPR-Cas, Tn7-like transposon, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.42
Radius of gyration Rg (electron density) rg_electron43.10
Forward intensity I(0) i01174720000.00
Molecular weight molecular_weight271910.0 kDa
Excluded volume excluded_volume336190 ų
Envelope volume envelope_volume460050 ų
Hydration-shell volume shell_volume85171 ų
Envelope diameter envelope_diameter131.8
Shell Rg shell_rg50.97
Envelope Rg envelope_rg42.52
Shape Rg shape_rg43.12
Total Rg total_rg43.37
Total atoms total_atoms19002
Residues n_residues2317
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 dmax131.3
Rg (real space) rg_real43.15
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real1.1750e+09
I(0) uncertainty (real space) i0_real_error2.0600e+07
Rg (reciprocal space) rg_reciprocal43.42
I(0) (reciprocal space) i0_reciprocal1175000000.0000
Solution quality estimate total_estimate0.8917
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.7
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha71210000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.807

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 7 domains

CATH v4.4 (7 domains)

Domain ID domain_id8bd4A01
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_id8bd4B01
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_id8bd4C01
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_id8bd4D01
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_id8bd4E01
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_id8bd4F01
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_id8bd4G01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)