9ut1

The helicase-primase complex from HHV1 bound with ssDNA and amenamevir

Method: ELECTRON MICROSCOPY Dmax: 190.9 Å Quality: REASONABLE

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

DNA replication helicase

Human alphaherpesvirus 1

UniProt P10189

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 DNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–882 Not recorded Ubiquitin-like protein SMT3,DNA primase × 1 (Q12306,P10236) Ubiquitin-like protein SMT3,DNA helicase/primase complex-associated protein × 1 (Q12306,P10192) synthetic DNA × 1 A1BXD Amenamevir × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HELI_HHV11
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 53–934; UniProt 1–882

Ubiquitin-like protein SMT3,DNA primase

Human alphaherpesvirus 1

UniProt P10236

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 DNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 1–1058 Mutation:R64T/R71E DNA replication helicase × 1 (P10189) Ubiquitin-like protein SMT3,DNA helicase/primase complex-associated protein × 1 (Q12306,P10192) synthetic DNA × 1 A1BXD Amenamevir × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRIM_HHV11
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 138–1195; UniProt 1–1058

Ubiquitin-like protein SMT3,DNA primase

Human alphaherpesvirus 1

UniProt Q12306

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 DNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 3–98 Chain C; UniProt 3–98 Mutation:R64T/R71E DNA replication helicase × 1 (P10189) synthetic DNA × 1 A1BXD Amenamevir × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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.

95 other PDB entries and 116 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMT3_YEAST
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain B; PDBConstruct 42–137; UniProt 3–98 Author chain C; PDBConstruct 42–137; UniProt 3–98

Ubiquitin-like protein SMT3,DNA helicase/primase complex-associated protein

Human alphaherpesvirus 1

UniProt P10192

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 DNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain C; UniProt 1–750 Mutation:R64T/R71E DNA replication helicase × 1 (P10189) Ubiquitin-like protein SMT3,DNA primase × 1 (Q12306,P10236) synthetic DNA × 1 A1BXD Amenamevir × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEPA_HHV11
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 138–887; UniProt 1–750

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 9ut1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ut1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ut1
Deposition date deposition_date2025-05-02
Structure title titleThe helicase-primase complex from HHV1 bound with ssDNA and amenamevir
Keywords keywordsHelicase, Primase, Inhibitor Complex, Herpesvirus, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.47
Radius of gyration Rg (electron density) rg_electron55.88
Forward intensity I(0) i02066450000.00
Molecular weight molecular_weight250260.0 kDa
Excluded volume excluded_volume241310 ų
Envelope volume envelope_volume506540 ų
Hydration-shell volume shell_volume79886 ų
Envelope diameter envelope_diameter195.5
Shell Rg shell_rg53.93
Envelope Rg envelope_rg54.28
Shape Rg shape_rg55.92
Total Rg total_rg55.77
Total atoms total_atoms18986
Residues n_residues2443
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 dmax190.9
Rg (real space) rg_real55.85
Rg uncertainty (real space) rg_real_error2.01
I(0) (real space) i0_real2.0660e+09
I(0) uncertainty (real space) i0_real_error4.6600e+07
Rg (reciprocal space) rg_reciprocal55.13
I(0) (reciprocal space) i0_reciprocal2064000000.0000
Solution quality estimate total_estimate0.5551
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.469
Kurtosis Kurtosis kurtosis-0.504
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha70570000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.763; Stabil: 1.000; Sysdev: 0.003; Positv: 1.000; Valcen: 0.914; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)