7lbq

Crystal structure of human Survivin bound to histone H3 T3phK4me2 peptide

Method: X-RAY DIFFRACTION Dmax: 50.8 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 1–142 Not recorded histone H3 T3phK4me2 peptide × 2 (P68431) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;1 uL of protein was mixed with 1uL of buffer composed of 2.25 mM spermine, 9 mM MgCl2, 0.9 mM spermidine, 1.8 mM cobalt (III)hexamine chloride, 0.05 sodium cacodylate pH 7.0, 5% PEG 400 Resolution 2.69 Å R-free 0.268

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 5–146; UniProt 1–142

histone H3 T3phK4me2 peptide

OrganismNot specified

UniProt P68431

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 E; UniProt 2–13 Non-standard monomer:Yes (specific site not provided by mmCIF) Baculoviral IAP repeat-containing protein 5 × 2 (O15392) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;289 K;1 uL of protein was mixed with 1uL of buffer composed of 2.25 mM spermine, 9 mM MgCl2, 0.9 mM spermidine, 1.8 mM cobalt (III)hexamine chloride, 0.05 sodium cacodylate pH 7.0, 5% PEG 400 Resolution 2.69 Å R-free 0.268

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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–12; UniProt 2–13

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 7lbq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7lbq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7lbq
Deposition date deposition_date2021-01-08
Structure title titleCrystal structure of human Survivin bound to histone H3 T3phK4me2 peptide
Keywords keywordslysine methylation, threonine phosphorylation, histone H3, CPC, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.11
Radius of gyration Rg (electron density) rg_electron18.16
Forward intensity I(0) i04426350.00
Molecular weight molecular_weight14996.0 kDa
Excluded volume excluded_volume18684 ų
Envelope volume envelope_volume22844 ų
Hydration-shell volume shell_volume12107 ų
Envelope diameter envelope_diameter73.4
Shell Rg shell_rg21.98
Envelope Rg envelope_rg19.15
Shape Rg shape_rg18.19
Total Rg total_rg18.79
Total atoms total_atoms1053
Residues n_residues136
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 dmax50.8
Rg (real space) rg_real16.85
Rg uncertainty (real space) rg_real_error0.11
I(0) (real space) i0_real4.2250e+06
I(0) uncertainty (real space) i0_real_error4.1620e+04
Rg (reciprocal space) rg_reciprocal18.44
I(0) (reciprocal space) i0_reciprocal4426000.0000
Solution quality estimate total_estimate0.6718
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.5
Skewness Skewness skewness0.479
Kurtosis Kurtosis kurtosis-0.165
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha2.3860
Highest regularization parameter α highest_alpha490100.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.922; Stabil: 0.992; Sysdev: 0.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)