3al3

Crystal Structure of TopBP1 BRCT7/8-BACH1 peptide complex

Method: X-RAY DIFFRACTION Dmax: 64.8 Å Quality: REASONABLE

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

DNA topoisomerase 2-binding protein 1

Homo sapiens

UniProt Q92547

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1264–1493 Fragment:BRCT7 and BRCT8, UNP residues 1264-1493 Peptide of Fanconi anemia group J protein × 1 (Q9BX63) FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;Sodium formate, pH 8, vapor diffusion, hanging drop, temperature 298K Resolution 2.15 Å R-free 0.236

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.

14 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOPB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–235; UniProt 1264–1493

Peptide of Fanconi anemia group J protein

OrganismNot specified

UniProt Q9BX63

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1129–1138 Fragment:UNP residues 1129-1138 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA topoisomerase 2-binding protein 1 × 1 (Q92547) FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;Sodium formate, pH 8, vapor diffusion, hanging drop, temperature 298K Resolution 2.15 Å R-free 0.236

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FANCJ_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 1129–1138

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 3al3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3al3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3al3
Deposition date deposition_date2010-07-22
Structure title titleCrystal Structure of TopBP1 BRCT7/8-BACH1 peptide complex
Keywords keywordsBRCT domain-phosphopeptide complex, DNA BINDING PROTEIN-PROTEIN BINDING complex; DNA BINDING PROTEIN/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.35
Radius of gyration Rg (electron density) rg_electron18.48
Forward intensity I(0) i012091100.00
Molecular weight molecular_weight25903.0 kDa
Excluded volume excluded_volume32420 ų
Envelope volume envelope_volume37377 ų
Hydration-shell volume shell_volume17411 ų
Envelope diameter envelope_diameter66.0
Shell Rg shell_rg24.05
Envelope Rg envelope_rg18.78
Shape Rg shape_rg18.47
Total Rg total_rg19.38
Total atoms total_atoms1826
Residues n_residues227
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 dmax64.8
Rg (real space) rg_real19.36
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.2090e+07
I(0) uncertainty (real space) i0_real_error1.4560e+05
Rg (reciprocal space) rg_reciprocal19.36
I(0) (reciprocal space) i0_reciprocal12090000.0000
Solution quality estimate total_estimate0.6150
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.421
Kurtosis Kurtosis kurtosis-0.136
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3316000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 1.000; Sysdev: 0.226; Positv: 1.000; Valcen: 0.976; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3al3A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10190 — BRCT domain
Domain ID domain_id3al3A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10190 — BRCT domain

8. Citations (1)

9. Files and Curves (10)