6n7w

Structure of bacteriophage T7 leading-strand DNA polymerase (D5A/E7A)/Trx in complex with a DNA fork and incoming dTTP (from multiple lead complexes)

Method: ELECTRON MICROSCOPY Dmax: 119.9 Å Quality: GOOD

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

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 Protein–DNA Heteromer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain H; UniProt 1–704 Mutation:D5A, E7A TrxA × 1 (Q14F07) DNA (25-MER) × 1 DNA (77-MER) × 1 MG MAGNESIUM ION × 1 TTP THYMIDINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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 1
Chains and sequence ranges Author chain H; PDBConstruct 1–704; UniProt 1–704

TrxA

Escherichia coli

UniProt Q14F07

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 × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain I; UniProt 36–144 Not recorded DNA-directed DNA polymerase × 1 (P00581) DNA (25-MER) × 1 DNA (77-MER) × 1 MG MAGNESIUM ION × 1 TTP THYMIDINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

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

View Construct and Data Evidence
UniProt name Q14F07_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–109; UniProt 36–144

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 6n7w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n7w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n7w
Deposition date deposition_date2018-11-28
Structure title titleStructure of bacteriophage T7 leading-strand DNA polymerase (D5A/E7A)/Trx in complex with a DNA fork and incoming dTTP (from multiple lead complexes)
Keywords keywordsDNA polymerase, helicase, DNA replication, replisome, TRANSFERASE-DNA complex; TRANSFERASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.62
Radius of gyration Rg (electron density) rg_electron36.17
Forward intensity I(0) i0249389000.00
Molecular weight molecular_weight112500.0 kDa
Excluded volume excluded_volume134520 ų
Envelope volume envelope_volume199760 ų
Hydration-shell volume shell_volume47125 ų
Envelope diameter envelope_diameter120.0
Shell Rg shell_rg41.52
Envelope Rg envelope_rg35.66
Shape Rg shape_rg36.15
Total Rg total_rg36.60
Total atoms total_atoms7837
Residues n_residues877
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 dmax119.9
Rg (real space) rg_real36.61
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real2.4940e+08
I(0) uncertainty (real space) i0_real_error4.0590e+06
Rg (reciprocal space) rg_reciprocal36.62
I(0) (reciprocal space) i0_reciprocal249400000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.8
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21770000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)