6n9v

Structure of bacteriophage T7 lagging-strand DNA polymerase (D5A/E7A) and gp4 (helicase/primase) bound to DNA including RNA/DNA hybrid, and an incoming dTTP (LagS1)

Method: ELECTRON MICROSCOPY Dmax: 188.8 Å Quality: GOOD

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

DNA primase/helicase

Enterobacteria phage T7

UniProt P03692

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 7 DNA 1 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain A; UniProt 1–566 Chain B; UniProt 1–566 Chain C; UniProt 1–566 Chain D; UniProt 1–566 Chain E; UniProt 1–566 Chain F; UniProt 1–566 Mutation:E343Q DNA-directed DNA polymerase × 1 (P00581) Primer × 1 Template × 1 TTP THYMIDINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 7 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRIM_BPT7
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–566; UniProt 1–566 Author chain B; PDBConstruct 1–566; UniProt 1–566 Author chain C; PDBConstruct 1–566; UniProt 1–566 Author chain D; PDBConstruct 1–566; UniProt 1–566 Author chain E; PDBConstruct 1–566; UniProt 1–566 Author chain F; PDBConstruct 1–566; UniProt 1–566

DNA-directed DNA polymerase

Enterobacteria phage T7

UniProt P00581

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 7 DNA 1 RNA 1 PDB declaration: nonameric(9) Consistent with all polymer counts Chain H; UniProt 1–704 Mutation:D5A, E7A DNA primase/helicase × 6 (P03692) Primer × 1 Template × 1 TTP THYMIDINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 7 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

23 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOL_BPT7
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–704; UniProt 1–704

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 6n9v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n9v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n9v
Deposition date deposition_date2018-12-04
Structure title titleStructure of bacteriophage T7 lagging-strand DNA polymerase (D5A/E7A) and gp4 (helicase/primase) bound to DNA including RNA/DNA hybrid, and an incoming dTTP (LagS1)
Keywords keywordsDNA polymerase, primase, helicase, DNA replication, replisome, HYDROLASE, TRANSFERASE-DNA complex; HYDROLASE,TRANSFERASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.70
Radius of gyration Rg (electron density) rg_electron55.67
Forward intensity I(0) i01460870000.00
Molecular weight molecular_weight307690.0 kDa
Excluded volume excluded_volume380550 ų
Envelope volume envelope_volume585190 ų
Hydration-shell volume shell_volume89520 ų
Envelope diameter envelope_diameter187.8
Shell Rg shell_rg56.76
Envelope Rg envelope_rg53.72
Shape Rg shape_rg55.72
Total Rg total_rg55.53
Total atoms total_atoms21526
Residues n_residues2683
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 dmax188.8
Rg (real space) rg_real55.85
Rg uncertainty (real space) rg_real_error2.14
I(0) (real space) i0_real1.4610e+09
I(0) uncertainty (real space) i0_real_error2.9850e+07
Rg (reciprocal space) rg_reciprocal55.54
I(0) (reciprocal space) i0_reciprocal1460000000.0000
Solution quality estimate total_estimate0.8632
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.7
Skewness Skewness skewness0.357
Kurtosis Kurtosis kurtosis-0.527
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha96290000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.591

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 7 domains

CATH v4.4 (7 domains)

Domain ID domain_id6n9vA00
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_id6n9vB00
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_id6n9vC00
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_id6n9vD00
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_id6n9vE01
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_id6n9vF02
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_id6n9vH01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily10 — Ribonuclease H-like superfamily/Ribonuclease H

8. Citations (1)

9. Files and Curves (10)