1a35

HUMAN TOPOISOMERASE I/DNA COMPLEX

Method: X-RAY DIFFRACTION Dmax: 82.3 Å Quality: EXCELLENT

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

PROTEIN (DNA TOPOISOMERASE I)

Homo sapiens

UniProt P11387

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 175–765 Fragment:CORE DOMAIN AND C-TERMINAL DOMAIN Mutation:Y723F ;DNA (5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*TP*AP*GP*AP*AP*AP*AP*AP*(BRU)P*(BRU)P*TP*TP*T)-3') ; × 1 ;DNA (5'-D(*AP*AP*AP*AP*AP*TP*+UP*+UP*+UP*+UP*CP*+UP*AP*AP*GP*TP*CP*TP*TP*TP*+ UP*T)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.7;295 K;pH 7.70, VAPOR DIFFUSION, SITTING DROP, temperature 295.00K Resolution 2.50 Å R-free 0.308

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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOP1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–591; UniProt 175–765

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 1a35

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a35
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a35
Deposition date deposition_date1998-01-29
Structure title titleHUMAN TOPOISOMERASE I/DNA COMPLEX
Keywords keywordsTOPOISOMERASE I/DNA), DNA, TOPOISOMERASE I, ISOMERASE-DNA COMPLEX; ISOMERASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.04
Radius of gyration Rg (electron density) rg_electron25.85
Forward intensity I(0) i093842500.00
Molecular weight molecular_weight67633.0 kDa
Excluded volume excluded_volume80876 ų
Envelope volume envelope_volume101900 ų
Hydration-shell volume shell_volume32693 ų
Envelope diameter envelope_diameter86.7
Shell Rg shell_rg33.31
Envelope Rg envelope_rg25.80
Shape Rg shape_rg25.88
Total Rg total_rg26.45
Total atoms total_atoms4674
Residues n_residues510
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 dmax82.3
Rg (real space) rg_real25.93
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real9.3840e+07
I(0) uncertainty (real space) i0_real_error1.2390e+06
Rg (reciprocal space) rg_reciprocal25.96
I(0) (reciprocal space) i0_reciprocal93840000.0000
Solution quality estimate total_estimate0.9028
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha10030000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; 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 (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1a35a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.163 — DNA breaking-rejoining enzymes
Superfamily Superfamily superfamilyd.163.1 — DNA breaking-rejoining enzymes
Family Family familyd.163.1.2 — Eukaryotic DNA topoisomerase I, catalytic core
Domain ID domain_idd1a35a2
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.15 — Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment
Superfamily Superfamily superfamilye.15.1 — Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment
Family Family familye.15.1.1 — Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment

CATH v4.4 (4 domains)

Domain ID domain_id1a35A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily41 — Yeast DNA topoisomerase - domain 1
Domain ID domain_id1a35A02
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology11 — DNA Topoisomerase I; domain 2
Homologous superfamily homologous superfamily10 — DNA Topoisomerase I, domain 2
Domain ID domain_id1a35A03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology15 — Topoisomerase I; Chain A, domain 3
Homologous superfamily homologous superfamily10 — Topoisomerase I; Chain A, domain 3
Domain ID domain_id1a35A04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology132 — Topoisomerase I; Chain A, domain 4
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)