1dew

CRYSTAL STRUCTURE OF HUMAN APE1 BOUND TO ABASIC DNA

Method: X-RAY DIFFRACTION Dmax: 101.9 Å Quality: GOOD

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

MAJOR APURINIC/APYRIMIDINIC ENDONUCLEASE

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 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain B; UniProt 39–317 Fragment:APE1 5'-D(*GP*CP*GP*TP*CP*CP*(3DR)P*CP*GP*AP*CP*GP*AP*CP*G)-3' × 1 5'-D(*GP*TP*CP*GP*TP*CP*GP*GP*GP*GP*AP*CP*GP*C)-3' × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;MPEG 2000, LITHIUM SULFATE, CACODYLATE BUFFER, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.65 Å R-free 0.286
2 Protein–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 39–317 Fragment:APE1 5'-D(*GP*CP*GP*TP*CP*CP*(3DR)P*CP*GP*AP*CP*GP*AP*CP*G)-3' × 1 5'-D(*GP*TP*CP*GP*TP*CP*GP*GP*GP*GP*AP*CP*GP*C)-3' × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;MPEG 2000, LITHIUM SULFATE, CACODYLATE BUFFER, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.65 Å R-free 0.286

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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–279; UniProt 39–317 Author chain B; PDBConstruct 1–279; UniProt 39–317

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 1dew

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1dew
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1dew
Deposition date deposition_date1999-11-15
Structure title titleCRYSTAL STRUCTURE OF HUMAN APE1 BOUND TO ABASIC DNA
Keywords keywordsENZYME:DNA COMPLEX, DNA REPAIR, ABASIC SITE, 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_guinier31.99
Radius of gyration Rg (electron density) rg_electron31.16
Forward intensity I(0) i0132343000.00
Molecular weight molecular_weight80281.0 kDa
Excluded volume excluded_volume95529 ų
Envelope volume envelope_volume124630 ų
Hydration-shell volume shell_volume33595 ų
Envelope diameter envelope_diameter104.9
Shell Rg shell_rg38.00
Envelope Rg envelope_rg30.88
Shape Rg shape_rg31.11
Total Rg total_rg31.82
Total atoms total_atoms5590
Residues n_residues613
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 dmax101.9
Rg (real space) rg_real32.03
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.3230e+08
I(0) uncertainty (real space) i0_real_error2.0290e+06
Rg (reciprocal space) rg_reciprocal32.02
I(0) (reciprocal space) i0_reciprocal132300000.0000
Solution quality estimate total_estimate0.8972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.6
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.703
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18810000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.903

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dewa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.151 — DNase I-like
Superfamily Superfamily superfamilyd.151.1 — DNase I-like
Family Family familyd.151.1.1 — DNase I-like
Domain ID domain_idd1dewb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.151 — DNase I-like
Superfamily Superfamily superfamilyd.151.1 — DNase I-like
Family Family familyd.151.1.1 — DNase I-like

CATH v4.4 (2 domains)

Domain ID domain_id1dewA00
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_id1dewB00
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)