6w3u

APE1 exonuclease substrate complex R237C

Method: X-RAY DIFFRACTION Dmax: 105.7 Å Quality: GOOD

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 3 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 43–318 Mutation:R237C ;DNA (5'-D(P*TP*CP*GP*AP*CP*GP*GP*AP*TP*CP*C)-3') ; × 1 ;DNA (5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*(C7R))-3') ; × 1 ;DNA (5'-D(*GP*GP*AP*TP*CP*CP*GP*TP*CP*GP*AP*TP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3') ; × 1 CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;7% PEG20000, 100 mM sodium citrate, 15% glycerol, 5 mM calcium chloride Resolution 2.40 Å R-free 0.250
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 43–318 Mutation:R237C EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;7% PEG20000, 100 mM sodium citrate, 15% glycerol, 5 mM calcium chloride Resolution 2.40 Å R-free 0.250

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 4
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 6w3u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6w3u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6w3u
Deposition date deposition_date2020-03-09
Structure title titleAPE1 exonuclease substrate complex R237C
Keywords keywordsnuclease, abasic site, DNA repair, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.81
Radius of gyration Rg (electron density) rg_electron30.24
Forward intensity I(0) i0108553000.00
Molecular weight molecular_weight74991.0 kDa
Excluded volume excluded_volume90458 ų
Envelope volume envelope_volume114980 ų
Hydration-shell volume shell_volume32616 ų
Envelope diameter envelope_diameter111.0
Shell Rg shell_rg36.09
Envelope Rg envelope_rg30.63
Shape Rg shape_rg30.14
Total Rg total_rg31.00
Total atoms total_atoms5229
Residues n_residues593
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 dmax105.7
Rg (real space) rg_real31.96
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real1.0860e+08
I(0) uncertainty (real space) i0_real_error1.9490e+06
Rg (reciprocal space) rg_reciprocal31.90
I(0) (reciprocal space) i0_reciprocal108500000.0000
Solution quality estimate total_estimate0.8738
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.363
Kurtosis Kurtosis kurtosis-0.589
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14710000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.907; Smooth: 0.899

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6w3uA00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology10 — Deoxyribonuclease I; Chain A
Homologous superfamily homologous superfamily10 — Endonuclease/exonuclease/phosphatase
Domain ID domain_id6w3uB00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology10 — Deoxyribonuclease I; Chain A
Homologous superfamily homologous superfamily10 — Endonuclease/exonuclease/phosphatase

8. Citations (1)

9. Files and Curves (10)