8p9c

Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with darpin 1810 F11

Method: X-RAY DIFFRACTION Dmax: 71.3 Å Quality: REASONABLE

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

Tumor protein 63

Homo sapiens

UniProt Q9H3D4

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 397–455 Not recorded Tumor protein p73 × 2 (O15350) Darpin 1810 F11 × 2 EDO 1,2-ETHANEDIOL × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293.15 K;0.2M ammonium acetate, 25% PEG3350, 0.1M HEPES pH 7.5 Resolution 1.76 Å R-free 0.210

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.

25 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name P63_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–61; UniProt 397–455

Tumor protein p73

Homo sapiens

UniProt O15350

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 351–398 Not recorded Tumor protein 63 × 2 (Q9H3D4) Darpin 1810 F11 × 2 EDO 1,2-ETHANEDIOL × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293.15 K;0.2M ammonium acetate, 25% PEG3350, 0.1M HEPES pH 7.5 Resolution 1.76 Å R-free 0.210

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.

27 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name P73_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–50; UniProt 351–398

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 8p9c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p9c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p9c
Deposition date deposition_date2023-06-05
Structure title titleCrystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with darpin 1810 F11
Keywords keywords;p63, p73, tetramerization domain, darpin, heterotetramer, Structural Genomics, Structural Genomics Consortium, SGC, DNA BINDING PROTEIN ;; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.12
Radius of gyration Rg (electron density) rg_electron20.14
Forward intensity I(0) i015448100.00
Molecular weight molecular_weight29346.0 kDa
Excluded volume excluded_volume36717 ų
Envelope volume envelope_volume46141 ų
Hydration-shell volume shell_volume19401 ų
Envelope diameter envelope_diameter71.2
Shell Rg shell_rg26.45
Envelope Rg envelope_rg20.97
Shape Rg shape_rg20.13
Total Rg total_rg21.11
Total atoms total_atoms2063
Residues n_residues259
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 dmax71.3
Rg (real space) rg_real21.10
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.5450e+07
I(0) uncertainty (real space) i0_real_error1.9650e+05
Rg (reciprocal space) rg_reciprocal21.10
I(0) (reciprocal space) i0_reciprocal15450000.0000
Solution quality estimate total_estimate0.7053
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.316
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3195000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 1.000; Sysdev: 0.225; Positv: 1.000; Valcen: 0.978; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)