1fn7

COUPLING OF DAMAGE RECOGNITION AND CATALYSIS BY A HUMAN BASE-EXCISION DNA REPAIR PROTEIN

Method: X-RAY DIFFRACTION Dmax: 74.0 Å Quality: GOOD

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

8-OXOGUANINE DNA GLYCOSYLASE 1

Homo sapiens

UniProt O15527

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 A; UniProt 12–325 Not recorded ;DNA (5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3') ; × 1 ;DNA (5'-D(*GP*CP*GP*TP*CP*CP*AP*(3DR)P*GP*TP*CP*TP*AP*CP*C)-3') ; × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;100 mM sodium cacodylate pH 6.5, 200 mM calcium acetate, 16-18% PEG, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.60 Å R-free 0.270

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.

46 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OGG1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–317; UniProt 12–325

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 1fn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1fn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1fn7
Deposition date deposition_date2000-08-21
Structure title titleCOUPLING OF DAMAGE RECOGNITION AND CATALYSIS BY A HUMAN BASE-EXCISION DNA REPAIR PROTEIN
Keywords keywords;DNA REPAIR, DNA GLYCOSYLASE, PROTEIN/DNA, Helix hairpin helix, base recognition, oxoguanine, hydroxyguanine, base flipping, flipped-out base, extrahelical DNA, mechanism-based inhibitor, base-exicision repair, AP lyase, DNA glycosidase, HYDROLASE-DNA COMPLEX ;; HYDROLASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.78
Radius of gyration Rg (electron density) rg_electron21.46
Forward intensity I(0) i041303900.00
Molecular weight molecular_weight43595.0 kDa
Excluded volume excluded_volume51866 ų
Envelope volume envelope_volume63225 ų
Hydration-shell volume shell_volume24455 ų
Envelope diameter envelope_diameter75.2
Shell Rg shell_rg28.50
Envelope Rg envelope_rg21.64
Shape Rg shape_rg21.44
Total Rg total_rg22.30
Total atoms total_atoms3038
Residues n_residues343
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 dmax74.0
Rg (real space) rg_real22.67
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real4.1300e+07
I(0) uncertainty (real space) i0_real_error5.6430e+05
Rg (reciprocal space) rg_reciprocal22.70
I(0) (reciprocal space) i0_reciprocal41300000.0000
Solution quality estimate total_estimate0.8923
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.187
Kurtosis Kurtosis kurtosis-0.372
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5230000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fn7a1
Class classa — All alpha proteins
Fold Fold folda.96 — DNA-glycosylase
Superfamily Superfamily superfamilya.96.1 — DNA-glycosylase
Family Family familya.96.1.3 — DNA repair glycosylase, 2 C-terminal domains
Domain ID domain_idd1fn7a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.129 — TBP-like
Superfamily Superfamily superfamilyd.129.1 — TATA-box binding protein-like
Family Family familyd.129.1.2 — DNA repair glycosylase, N-terminal domain

CATH v4.4 (3 domains)

Domain ID domain_id1fn7A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily40
Domain ID domain_id1fn7A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1670 — Endonuclease Iii, domain 2
Homologous superfamily homologous superfamily10 — Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal)
Domain ID domain_id1fn7A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology340 — Endonuclease III; domain 1
Homologous superfamily homologous superfamily30 — Hypothetical protein; domain 2

8. Citations (2)

9. Files and Curves (10)