4qh9

Crystal structure of Mn2+ bound human APE1

Method: X-RAY DIFFRACTION Dmax: 56.0 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 38–318 Fragment:UNP residues 38-318 Mutation:C138A EDO 1,2-ETHANEDIOL × 7 MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;0.1M MES, 0.2M Sodium Chloride, 19% PEG 3350, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.17 Å R-free 0.256

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 5–285; UniProt 38–318

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 4qh9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qh9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4qh9
Deposition date deposition_date2014-05-27
Structure title titleCrystal structure of Mn2+ bound human APE1
Keywords keywordsBeta Sandwich, Endonuclease, DNA-binding, Nucleus, LYASE; LYASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.82
Radius of gyration Rg (electron density) rg_electron17.65
Forward intensity I(0) i017500000.00
Molecular weight molecular_weight32046.0 kDa
Excluded volume excluded_volume40237 ų
Envelope volume envelope_volume44696 ų
Hydration-shell volume shell_volume20370 ų
Envelope diameter envelope_diameter55.2
Shell Rg shell_rg24.59
Envelope Rg envelope_rg17.99
Shape Rg shape_rg17.61
Total Rg total_rg18.73
Total atoms total_atoms2257
Residues n_residues281
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 dmax56.0
Rg (real space) rg_real18.66
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real1.7500e+07
I(0) uncertainty (real space) i0_real_error1.8490e+05
Rg (reciprocal space) rg_reciprocal18.68
I(0) (reciprocal space) i0_reciprocal17500000.0000
Solution quality estimate total_estimate0.9043
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.041
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4036000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4qh9a_
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 (1 domains)

Domain ID domain_id4qh9A00
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)