6x0m

Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin

Method: ELECTRON MICROSCOPY Dmax: 156.0 Å Quality: GOOD

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

Histone PARylation factor 1

Homo sapiens

UniProt Q9NWY4

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 4 PDB declaration: octameric(8) Consistent with all polymer counts Chain O; UniProt 1–346 Chain o; UniProt 1–346 Not recorded Poly [ADP-ribose] polymerase 2 × 2 (Q9UGN5) DNA (167-MER) × 2 DNA (167-MER) × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.30 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.

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

View Construct and Data Evidence
UniProt name HPF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain O; PDBConstruct 11–356; UniProt 1–346 Author chain o; PDBConstruct 11–356; UniProt 1–346

Poly [ADP-ribose] polymerase 2

Homo sapiens

UniProt Q9UGN5

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 4 PDB declaration: octameric(8) Consistent with all polymer counts Chain P; UniProt 1–570 Chain p; UniProt 1–570 Not recorded Histone PARylation factor 1 × 2 (Q9NWY4) DNA (167-MER) × 2 DNA (167-MER) × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.30 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.

29 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PARP2_HUMAN
Isoform Q9UGN5-2
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 21–590; UniProt 1–570 Author chain p; PDBConstruct 21–590; UniProt 1–570

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 6x0m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6x0m
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6x0m
Deposition date deposition_date2020-05-16
Structure title titleBridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin
Keywords keywordsDNA repair, PARP1, PARP2, HPF1, ADP-ribosylation, chromatin, histone modifications, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.34
Radius of gyration Rg (electron density) rg_electron46.55
Forward intensity I(0) i0507966000.00
Molecular weight molecular_weight177470.0 kDa
Excluded volume excluded_volume218610 ų
Envelope volume envelope_volume315990 ų
Hydration-shell volume shell_volume59504 ų
Envelope diameter envelope_diameter151.3
Shell Rg shell_rg47.54
Envelope Rg envelope_rg45.30
Shape Rg shape_rg46.64
Total Rg total_rg46.31
Total atoms total_atoms12421
Residues n_residues1472
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 dmax156.0
Rg (real space) rg_real45.63
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real5.0800e+08
I(0) uncertainty (real space) i0_real_error9.3430e+06
Rg (reciprocal space) rg_reciprocal45.34
I(0) (reciprocal space) i0_reciprocal507800000.0000
Solution quality estimate total_estimate0.8420
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.448
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha69180000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.740; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.837; Smooth: 0.884

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)