9e5y

T4 Bacteriophage Replicative Polymerase Captured in Polymerase Exchange State 1

Method: ELECTRON MICROSCOPY Dmax: 145.7 Å Quality: GOOD

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

DNA-directed DNA polymerase

Escherichia phage T4

UniProt P04415

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain A; UniProt 1–898 Chain C; UniProt 1–898 Not recorded Sliding clamp × 3 (P04525) ;DNA (5'-AGC TAT GAC CAT GAT TAC GAA TTG ddC-3') ; × 1 DNA (38-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOL_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–898; UniProt 1–898 Author chain C; PDBConstruct 1–898; UniProt 1–898

Sliding clamp

Escherichia phage T4

UniProt P04525

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 × 5 DNA 2 PDB declaration: heptameric(7) Consistent with all polymer counts Chain B; UniProt 1–228 Chain D; UniProt 1–228 Chain E; UniProt 1–228 Not recorded DNA-directed DNA polymerase × 2 (P04415) ;DNA (5'-AGC TAT GAC CAT GAT TAC GAA TTG ddC-3') ; × 1 DNA (38-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CLAMP_BPT4
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–228; UniProt 1–228 Author chain D; PDBConstruct 1–228; UniProt 1–228 Author chain E; PDBConstruct 1–228; UniProt 1–228

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 9e5y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e5y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e5y
Deposition date deposition_date2024-10-28
Structure title titleT4 Bacteriophage Replicative Polymerase Captured in Polymerase Exchange State 1
Keywords keywordsreplication, T4, holoenzyme, replication-DNA complex; replication/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.17
Radius of gyration Rg (electron density) rg_electron47.93
Forward intensity I(0) i01342700000.00
Molecular weight molecular_weight298000.0 kDa
Excluded volume excluded_volume370030 ų
Envelope volume envelope_volume562460 ų
Hydration-shell volume shell_volume96048 ų
Envelope diameter envelope_diameter150.5
Shell Rg shell_rg54.78
Envelope Rg envelope_rg45.62
Shape Rg shape_rg47.94
Total Rg total_rg48.13
Total atoms total_atoms20896
Residues n_residues2533
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 dmax145.7
Rg (real space) rg_real47.85
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real1.3430e+09
I(0) uncertainty (real space) i0_real_error2.3100e+07
Rg (reciprocal space) rg_reciprocal48.17
I(0) (reciprocal space) i0_reciprocal1343000000.0000
Solution quality estimate total_estimate0.8890
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.4
Skewness Skewness skewness0.098
Kurtosis Kurtosis kurtosis-0.578
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha110700000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.959; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.709

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)