9mj5

Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA

Method: ELECTRON MICROSCOPY Dmax: 138.1 Å Quality: GOOD

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

Replication protein A 14 kDa subunit

Homo sapiens

UniProt P35244

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–121 Not recorded Replication protein A 32 kDa subunit × 1 (P15927) Replication protein A 70 kDa DNA-binding subunit × 1 (P27694) RNA-DNA primer (11-mer) × 1 DNA polymerase alpha catalytic subunit × 1 (P09884) DNA template (35-mer) × 1 ZN ZINC ION × 1 MG MAGNESIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

9 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFA3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–121; UniProt 1–121

Replication protein A 32 kDa subunit

Homo sapiens

UniProt P15927

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 35–270 Not recorded Replication protein A 14 kDa subunit × 1 (P35244) Replication protein A 70 kDa DNA-binding subunit × 1 (P27694) RNA-DNA primer (11-mer) × 1 DNA polymerase alpha catalytic subunit × 1 (P09884) DNA template (35-mer) × 1 ZN ZINC ION × 1 MG MAGNESIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

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

View Construct and Data Evidence
UniProt name RFA2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–236; UniProt 35–270

Replication protein A 70 kDa DNA-binding subunit

Homo sapiens

UniProt P27694

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 438–616 Not recorded Replication protein A 14 kDa subunit × 1 (P35244) Replication protein A 32 kDa subunit × 1 (P15927) RNA-DNA primer (11-mer) × 1 DNA polymerase alpha catalytic subunit × 1 (P09884) DNA template (35-mer) × 1 ZN ZINC ION × 1 MG MAGNESIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFA1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–179; UniProt 438–616

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain S; UniProt 335–1244 Not recorded Replication protein A 14 kDa subunit × 1 (P35244) Replication protein A 32 kDa subunit × 1 (P15927) Replication protein A 70 kDa DNA-binding subunit × 1 (P27694) RNA-DNA primer (11-mer) × 1 DNA template (35-mer) × 1 ZN ZINC ION × 1 MG MAGNESIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

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 5
Chains and sequence ranges Author chain S; PDBConstruct 1–910; UniProt 335–1244

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 9mj5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mj5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mj5
Deposition date deposition_date2024-12-13
Structure title titleCatalytic domain of human DNA polymerase alpha in complex with DNA and RPA
Keywords keywordsDNA replication, Replication-DNA-RNA complex; Replication/DNA/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.81
Radius of gyration Rg (electron density) rg_electron41.60
Forward intensity I(0) i0467948000.00
Molecular weight molecular_weight170520.0 kDa
Excluded volume excluded_volume210930 ų
Envelope volume envelope_volume313340 ų
Hydration-shell volume shell_volume63285 ų
Envelope diameter envelope_diameter138.8
Shell Rg shell_rg46.40
Envelope Rg envelope_rg40.74
Shape Rg shape_rg41.58
Total Rg total_rg41.93
Total atoms total_atoms11919
Residues n_residues1420
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 dmax138.1
Rg (real space) rg_real41.82
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real4.6790e+08
I(0) uncertainty (real space) i0_real_error8.5880e+06
Rg (reciprocal space) rg_reciprocal41.81
I(0) (reciprocal space) i0_reciprocal467900000.0000
Solution quality estimate total_estimate0.8775
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.2
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.425
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha82820000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.713

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)