7tc3

Human APE1 in the apo form

Method: X-RAY DIFFRACTION Dmax: 65.5 Å Quality: GOOD

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

DNA-(apurinic or apyrimidinic site) endonuclease, 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 39–318 Not recorded EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;PEG3350, Sodium Formate Resolution 1.25 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.

66 other PDB entries and 123 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 7–286; UniProt 39–318

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 7tc3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tc3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7tc3
Deposition date deposition_date2021-12-22
Structure title titleHuman APE1 in the apo form
Keywords keywordsAP Endonuclease1, APE1, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.77
Radius of gyration Rg (electron density) rg_electron17.55
Forward intensity I(0) i016663400.00
Molecular weight molecular_weight31302.0 kDa
Excluded volume excluded_volume39322 ų
Envelope volume envelope_volume43960 ų
Hydration-shell volume shell_volume20128 ų
Envelope diameter envelope_diameter61.5
Shell Rg shell_rg24.63
Envelope Rg envelope_rg18.04
Shape Rg shape_rg17.51
Total Rg total_rg18.69
Total atoms total_atoms2209
Residues n_residues282
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 dmax65.5
Rg (real space) rg_real18.63
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.6660e+07
I(0) uncertainty (real space) i0_real_error2.1690e+05
Rg (reciprocal space) rg_reciprocal18.65
I(0) (reciprocal space) i0_reciprocal16660000.0000
Solution quality estimate total_estimate0.7719
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.087
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4358000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.677; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)