7tr7

APE1 product complex with abasic ssDNA

Method: X-RAY DIFFRACTION Dmax: 89.7 Å Quality: REASONABLE

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

DNA-(apurinic or apyrimidinic site) lyase

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 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 43–318 Mutation:C138A ;DNA (5'-D(P*(3DR)P*CP*GP*AP*TP*GP*C)-3') ; × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;291 K;0.05M KCl, 0.05M sodium cacodylate pH 6, 10% PEG 8,000, 5mM spermine, 5mM L-Argininamide dihydrochloride Resolution 2.00 Å R-free 0.215
2 Protein–DNA Monomer Protein × 1 DNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain B; UniProt 43–318 Mutation:C138A ;DNA (5'-D(P*(3DR)P*CP*GP*AP*TP*GP*C)-3') ; × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;291 K;0.05M KCl, 0.05M sodium cacodylate pH 6, 10% PEG 8,000, 5mM spermine, 5mM L-Argininamide dihydrochloride Resolution 2.00 Å R-free 0.215

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 7tr7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tr7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7tr7
Deposition date deposition_date2022-01-28
Structure title titleAPE1 product complex with abasic ssDNA
Keywords keywordsDNA Repair, Abasic ssDNA, AP-Endonuclease, LYASE, LYASE-DNA complex; LYASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.14
Radius of gyration Rg (electron density) rg_electron26.95
Forward intensity I(0) i075469400.00
Molecular weight molecular_weight66134.0 kDa
Excluded volume excluded_volume81911 ų
Envelope volume envelope_volume99803 ų
Hydration-shell volume shell_volume31092 ų
Envelope diameter envelope_diameter93.0
Shell Rg shell_rg34.16
Envelope Rg envelope_rg27.10
Shape Rg shape_rg26.88
Total Rg total_rg27.86
Total atoms total_atoms4648
Residues n_residues564
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 dmax89.7
Rg (real space) rg_real28.16
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real7.5470e+07
I(0) uncertainty (real space) i0_real_error1.1890e+06
Rg (reciprocal space) rg_reciprocal28.16
I(0) (reciprocal space) i0_reciprocal75470000.0000
Solution quality estimate total_estimate0.6903
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha16250000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 0.109; Positv: 1.000; Valcen: 0.973; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)