9dp2

APE1 N174A Product Complex with Abasic DNA

Method: X-RAY DIFFRACTION Dmax: 107.0 Å Quality: GOOD

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

DNA repair nuclease/redox regulator APEX1, mitochondrial

Homo sapiens

UniProt P27695

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 Monomer Protein × 1 DNA 3 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 43–318 Mutation:tr1-42, C138A, N174A ;DNA (5'-D(P*(3DR)P*CP*GP*AP*CP*GP*GP*AP*TP*CP*C)-3') ; × 1 ;DNA (5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*C)-3') ; × 1 ;DNA (5'-D(*GP*GP*AP*TP*CP*CP*GP*TP*CP*GP*GP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3') ; × 1 MN MANGANESE (II) ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;100 mM sodium citrate, pH 5.0, 200 mM magnesium chloride, 16-21% PEG20000 Resolution 1.99 Å R-free 0.203
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 43–318 Mutation:tr1-42, C138A, N174A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;100 mM sodium citrate, pH 5.0, 200 mM magnesium chloride, 16-21% PEG20000 Resolution 1.99 Å R-free 0.203

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.

66 other PDB entries and 122 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APEX1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–276; UniProt 43–318 Author chain B; PDBConstruct 1–276; UniProt 43–318

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 9dp2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9dp2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9dp2
Deposition date deposition_date2024-09-20
Structure title titleAPE1 N174A Product Complex with Abasic DNA
Keywords keywordsAPE1, APEX1, Endonuclease, DNA Repair, HYDROLASE-DNA complex; HYDROLASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.70
Radius of gyration Rg (electron density) rg_electron29.60
Forward intensity I(0) i0104973000.00
Molecular weight molecular_weight73725.0 kDa
Excluded volume excluded_volume89057 ų
Envelope volume envelope_volume113420 ų
Hydration-shell volume shell_volume33110 ų
Envelope diameter envelope_diameter114.2
Shell Rg shell_rg35.45
Envelope Rg envelope_rg29.73
Shape Rg shape_rg29.54
Total Rg total_rg30.25
Total atoms total_atoms5148
Residues n_residues588
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 dmax107.0
Rg (real space) rg_real30.88
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real1.0500e+08
I(0) uncertainty (real space) i0_real_error1.8410e+06
Rg (reciprocal space) rg_reciprocal30.81
I(0) (reciprocal space) i0_reciprocal105000000.0000
Solution quality estimate total_estimate0.8503
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.9
Skewness Skewness skewness0.499
Kurtosis Kurtosis kurtosis-0.160
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14760000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.784; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.836; Smooth: 0.862

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)