1e9n

A second divalent metal ion in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1, and its implications for the catalytic mechanism

Method: X-RAY DIFFRACTION Dmax: 92.4 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–317 Not recorded PB LEAD (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;HANGING DROP, DROP 2+2 UL, 15MG/ML PROTEIN, 1 ML WELL, 0.1M TRIS-HCL, PH 7.5, 0.2M NAOAC, 30% PEG4K, 20MM HECAMEG, 1MM PB(OAC)2, 1MM DTT Resolution 2.20 Å R-free 0.252
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–317 Not recorded PB LEAD (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;HANGING DROP, DROP 2+2 UL, 15MG/ML PROTEIN, 1 ML WELL, 0.1M TRIS-HCL, PH 7.5, 0.2M NAOAC, 30% PEG4K, 20MM HECAMEG, 1MM PB(OAC)2, 1MM DTT Resolution 2.20 Å R-free 0.252

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 APE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–318; UniProt 1–317 Author chain B; PDBConstruct 2–318; UniProt 1–317

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 1e9n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1e9n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1e9n
Deposition date deposition_date2000-10-24
Structure title titleA second divalent metal ion in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1, and its implications for the catalytic mechanism
Keywords keywordsDNA REPAIR, DNA REPAIR ENDONUCLEASE, BASE EXCISION REPAIR, ABASIC ENDONUCLEASE, APE1, HAP1, REF-1, ALPHA, BETA SANDWICH; DNA REPAIR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.46
Radius of gyration Rg (electron density) rg_electron27.95
Forward intensity I(0) i064766900.00
Molecular weight molecular_weight62257.0 kDa
Excluded volume excluded_volume77298 ų
Envelope volume envelope_volume93101 ų
Hydration-shell volume shell_volume28711 ų
Envelope diameter envelope_diameter101.4
Shell Rg shell_rg34.15
Envelope Rg envelope_rg27.94
Shape Rg shape_rg27.94
Total Rg total_rg28.58
Total atoms total_atoms4340
Residues n_residues548
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 dmax92.4
Rg (real space) rg_real28.64
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real6.4770e+07
I(0) uncertainty (real space) i0_real_error1.0220e+06
Rg (reciprocal space) rg_reciprocal28.59
I(0) (reciprocal space) i0_reciprocal64760000.0000
Solution quality estimate total_estimate0.7812
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.412
Kurtosis Kurtosis kurtosis-0.605
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22900000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.770; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.849; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1e9na_
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_idd1e9nb_
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_id1e9nA00
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_id1e9nB00
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)