5n8a

Structure of RPA70N in complex with PrimPol (fragment 480-560)

Method: X-RAY DIFFRACTION Dmax: 51.3 Å Quality: GOOD

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

DNA-directed primase/polymerase protein

Homo sapiens

UniProt Q96LW4

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain X; UniProt 480–560 Fragment:UNP residues 479-559 Replication protein A 70 kDa DNA-binding subunit × 1 (P27694) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293.15 K;0.2M imidazole malate, 30% w/v PEG 4000 Resolution 1.28 Å R-free 0.178

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.

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

View Construct and Data Evidence
UniProt name PRIPO_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 22–102; UniProt 480–560

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–120 Mutation:E7R DNA-directed primase/polymerase protein × 1 (Q96LW4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293.15 K;0.2M imidazole malate, 30% w/v PEG 4000 Resolution 1.28 Å R-free 0.178

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 2
Chains and sequence ranges Author chain A; PDBConstruct 2–121; UniProt 1–120

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 5n8a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5n8a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5n8a
Deposition date deposition_date2017-02-23
Structure title titleStructure of RPA70N in complex with PrimPol (fragment 480-560)
Keywords keywordsComplex, Replication, Basic cleft, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.34
Radius of gyration Rg (electron density) rg_electron13.87
Forward intensity I(0) i03959960.00
Molecular weight molecular_weight14289.0 kDa
Excluded volume excluded_volume18063 ų
Envelope volume envelope_volume20196 ų
Hydration-shell volume shell_volume12337 ų
Envelope diameter envelope_diameter49.8
Shell Rg shell_rg19.72
Envelope Rg envelope_rg14.19
Shape Rg shape_rg13.88
Total Rg total_rg15.08
Total atoms total_atoms999
Residues n_residues130
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 dmax51.3
Rg (real space) rg_real15.22
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real3.9600e+06
I(0) uncertainty (real space) i0_real_error4.7780e+04
Rg (reciprocal space) rg_reciprocal15.23
I(0) (reciprocal space) i0_reciprocal3960000.0000
Solution quality estimate total_estimate0.8691
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.5
Skewness Skewness skewness0.101
Kurtosis Kurtosis kurtosis-0.372
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha865700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.765; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5n8aa1
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.3 — Single strand DNA-binding domain, SSB
Domain ID domain_idd5n8aa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id5n8aA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (1)

9. Files and Curves (10)