1bix

THE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES

Method: X-RAY DIFFRACTION Dmax: 55.5 Å Quality: EXCELLENT

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

AP ENDONUCLEASE 1

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 31–317 Not recorded SM SAMARIUM (III) ION × 4 PT PLATINUM (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.4;pH 7.4 Resolution 2.20 Å R-free 0.269

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 1–287; UniProt 31–317

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 1bix

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bix
Deposition date deposition_date1998-06-19
Structure title titleTHE CRYSTAL STRUCTURE OF THE HUMAN DNA REPAIR ENDONUCLEASE HAP1 SUGGESTS THE RECOGNITION OF EXTRA-HELICAL DEOXYRIBOSE AT DNA ABASIC SITES
Keywords keywordsDNA REPAIR, ENDONUCLEASE, HAP1, REF-1, ABASIC SITE RECOGNITION; DNA REPAIR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.94
Radius of gyration Rg (electron density) rg_electron17.57
Forward intensity I(0) i018588900.00
Molecular weight molecular_weight31831.0 kDa
Excluded volume excluded_volume39223 ų
Envelope volume envelope_volume43863 ų
Hydration-shell volume shell_volume20153 ų
Envelope diameter envelope_diameter56.0
Shell Rg shell_rg24.43
Envelope Rg envelope_rg17.86
Shape Rg shape_rg17.44
Total Rg total_rg18.87
Total atoms total_atoms2195
Residues n_residues275
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 dmax55.5
Rg (real space) rg_real18.77
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.8590e+07
I(0) uncertainty (real space) i0_real_error2.2820e+05
Rg (reciprocal space) rg_reciprocal18.80
I(0) (reciprocal space) i0_reciprocal18590000.0000
Solution quality estimate total_estimate0.9073
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.028
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3583000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.993

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_idd1bixa_
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_id1bixA00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology10 — Deoxyribonuclease I; Chain A
Homologous superfamily homologous superfamily10 — Endonuclease/exonuclease/phosphatase

8. Citations (2)

9. Files and Curves (10)