1de9

HUMAN APE1 ENDONUCLEASE WITH BOUND ABASIC DNA AND MN2+ ION

Method: X-RAY DIFFRACTION Dmax: 129.2 Å Quality: SUSPICIOUS

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 3 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 42–317 Fragment:APE1 5'-d(*CP*TP*AP*C)-3' × 1 5'-d(P*(3DR)P*GP*AP*TP*C)-3' × 1 5'-d(*GP*AP*TP*CP*GP*GP*TP*AP*G)-3' × 1 MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;MPEG 2000, LITHIUM SULFATE, MANGANESE CHLORIDE, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.00 Å R-free 0.274
2 Protein–DNA Monomer Protein × 1 DNA 3 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 42–317 Fragment:APE1 5'-d(*CP*TP*AP*C)-3' × 1 5'-d(P*(3DR)P*GP*AP*TP*C)-3' × 1 5'-d(*GP*AP*TP*CP*GP*GP*TP*AP*G)-3' × 1 MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;MPEG 2000, LITHIUM SULFATE, MANGANESE CHLORIDE, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.00 Å R-free 0.274

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 42–317 Author chain B; PDBConstruct 1–276; UniProt 42–317

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 1de9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1de9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1de9
Deposition date deposition_date1999-11-13
Structure title titleHUMAN APE1 ENDONUCLEASE WITH BOUND ABASIC DNA AND MN2+ ION
Keywords keywordsENZYME:DNA COMPLEX, DNA REPAIR ABASIC SITE, AP ENDONUCLEASE, 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_guinier39.76
Radius of gyration Rg (electron density) rg_electron39.21
Forward intensity I(0) i093946200.00
Molecular weight molecular_weight72792.0 kDa
Excluded volume excluded_volume88287 ų
Envelope volume envelope_volume119260 ų
Hydration-shell volume shell_volume25143 ų
Envelope diameter envelope_diameter130.4
Shell Rg shell_rg45.79
Envelope Rg envelope_rg37.92
Shape Rg shape_rg39.18
Total Rg total_rg39.64
Total atoms total_atoms5088
Residues n_residues586
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 dmax129.2
Rg (real space) rg_real40.30
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real9.3950e+07
I(0) uncertainty (real space) i0_real_error1.6130e+06
Rg (reciprocal space) rg_reciprocal39.99
I(0) (reciprocal space) i0_reciprocal93910000.0000
Solution quality estimate total_estimate0.4019
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-1.193
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17640000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.048; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.133; Smooth: 0.756

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_idd1de9a_
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_idd1de9b_
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_id1de9A00
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_id1de9B00
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)