8d96

Human DNA polymerase alpha/primase elongation complex I bound to primer/template

Method: ELECTRON MICROSCOPY Dmax: 126.7 Å Quality: GOOD

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

DNA primase large subunit

Homo sapiens

UniProt P49643

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 B; UniProt 1–509 Not recorded DNA polymerase alpha catalytic subunit × 1 (P09884) ;DNA/RNA (5'-GTP)-R(P*GP*CP*GP*GP*CP*AP*CP*G)-D(P*AP*CP*C)-3') ; × 1 ;DNA (5'-D(*AP*TP*AP*AP*TP*GP*GP*TP*CP*GP*TP*GP*CP*CP*GP*CP*CP*AP*AP*TP*AP*A)-3') ; × 1 SF4 IRON/SULFUR CLUSTER × 1 MG MAGNESIUM ION × 1 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is made fresh at 80 mM before added to the sample at a final concentration of 4-8 mM immediately before vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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.

21 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRI2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–509; UniProt 1–509

DNA polymerase alpha catalytic subunit

Homo sapiens

UniProt P09884

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 C; UniProt 1–1462 Not recorded DNA primase large subunit × 1 (P49643) ;DNA/RNA (5'-GTP)-R(P*GP*CP*GP*GP*CP*AP*CP*G)-D(P*AP*CP*C)-3') ; × 1 ;DNA (5'-D(*AP*TP*AP*AP*TP*GP*GP*TP*CP*GP*TP*GP*CP*CP*GP*CP*CP*AP*AP*TP*AP*A)-3') ; × 1 SF4 IRON/SULFUR CLUSTER × 1 MG MAGNESIUM ION × 1 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;CHAPSO is made fresh at 80 mM before added to the sample at a final concentration of 4-8 mM immediately before vitrification. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.35 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.

21 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOLA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1462; UniProt 1–1462

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 8d96

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8d96
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8d96
Deposition date deposition_date2022-06-09
Structure title titleHuman DNA polymerase alpha/primase elongation complex I bound to primer/template
Keywords keywordsDNA replication, human DNA polymerase alpha/primase, human primosome, elongation complex, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.81
Radius of gyration Rg (electron density) rg_electron38.00
Forward intensity I(0) i0282445000.00
Molecular weight molecular_weight131750.0 kDa
Excluded volume excluded_volume163160 ų
Envelope volume envelope_volume229510 ų
Hydration-shell volume shell_volume51231 ų
Envelope diameter envelope_diameter132.4
Shell Rg shell_rg43.13
Envelope Rg envelope_rg37.43
Shape Rg shape_rg37.99
Total Rg total_rg38.36
Total atoms total_atoms9203
Residues n_residues1086
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 dmax126.7
Rg (real space) rg_real37.86
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real2.8240e+08
I(0) uncertainty (real space) i0_real_error4.7820e+06
Rg (reciprocal space) rg_reciprocal37.83
I(0) (reciprocal space) i0_reciprocal282400000.0000
Solution quality estimate total_estimate0.8856
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.2
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.362
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha65540000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.870

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)