9tph

Survivin 1-127 in complex with a molecular tweezer-Histone-H3-peptide conjugate

Method: X-RAY DIFFRACTION Dmax: 81.1 Å Quality: REASONABLE

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

Baculoviral IAP repeat-containing protein 5

Homo sapiens

UniProt O15392

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–127 Chain B; UniProt 2–127 Not recorded Histone-H3-peptide conjugated to molecular tweezer × 2 ZN ZINC ION × 2 CA CALCIUM ION × 3 A1JXR Molecular tweezer (BIRC5) × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;277 K;0.1M imidazole pH 8.0, 0.05M Ca-acetate, 35% v/v 2-ethoxyethanol Resolution 2.00 Å R-free 0.263

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.

35 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BIRC5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–126; UniProt 2–127 Author chain B; PDBConstruct 1–126; UniProt 2–127

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 9tph

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9tph
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9tph
Deposition date deposition_date2025-12-18
最后修订 last_revision2026-04-15
Structure title titleSurvivin 1-127 in complex with a molecular tweezer-Histone-H3-peptide conjugate
Keywords keywords;protein-protein interactions, supramolecular ligands, molecular tweezers, peptide binding, BIR domain, zinc finger, chromosomal passenger complex, cell cycle, mitosis, apoptosis ;; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.72
Radius of gyration Rg (electron density) rg_electron22.56
Forward intensity I(0) i032156100.00
Molecular weight molecular_weight29251.0 kDa
Excluded volume excluded_volume28372 ų
Envelope volume envelope_volume49502 ų
Hydration-shell volume shell_volume19537 ų
Envelope diameter envelope_diameter82.5
Shell Rg shell_rg28.15
Envelope Rg envelope_rg23.07
Shape Rg shape_rg22.68
Total Rg total_rg22.95
Total atoms total_atoms2193
Residues n_residues248
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 dmax81.1
Rg (real space) rg_real22.90
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real3.2160e+07
I(0) uncertainty (real space) i0_real_error4.4390e+05
Rg (reciprocal space) rg_reciprocal22.86
I(0) (reciprocal space) i0_reciprocal32160000.0000
Solution quality estimate total_estimate0.6432
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.602
Kurtosis Kurtosis kurtosis-0.028
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8733000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.654; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.778; Smooth: 0.891

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)