3uik

crystal structure of human Survivin mutant K62Y/H80W in complex with H3(1-10) peptide

Method: X-RAY DIFFRACTION Dmax: 101.0 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 Chain B; UniProt 1–142 Fragment:unp residues 1-142 Mutation:K62Y, H80W, K139E histone H3(1-10) peptide × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.2 M succinic acid, pH 7.0, 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.281

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 2–143; UniProt 1–142 Author chain B; PDBConstruct 2–143; UniProt 1–142

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 3uik

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3uik
Deposition date deposition_date2011-11-04
Structure title titlecrystal structure of human Survivin mutant K62Y/H80W in complex with H3(1-10) peptide
Keywords keywordsBIR domain, mitosis, T3 phosphorylated H3 binding, Smac/Diablo binding, APOPTOSIS-APOPTOSIS INHIBITOR complex; APOPTOSIS/APOPTOSIS INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.09
Radius of gyration Rg (electron density) rg_electron27.75
Forward intensity I(0) i018364800.00
Molecular weight molecular_weight32606.0 kDa
Excluded volume excluded_volume40720 ų
Envelope volume envelope_volume54797 ų
Hydration-shell volume shell_volume18636 ų
Envelope diameter envelope_diameter110.5
Shell Rg shell_rg31.06
Envelope Rg envelope_rg28.32
Shape Rg shape_rg27.73
Total Rg total_rg28.22
Total atoms total_atoms2290
Residues n_residues278
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 dmax101.0
Rg (real space) rg_real28.46
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.8360e+07
I(0) uncertainty (real space) i0_real_error2.8070e+05
Rg (reciprocal space) rg_reciprocal28.35
I(0) (reciprocal space) i0_reciprocal18360000.0000
Solution quality estimate total_estimate0.6834
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.458
Kurtosis Kurtosis kurtosis-0.523
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2373000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.533; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.281; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3uika_
Class classg — Small proteins
Fold Fold foldg.52 — Inhibitor of apoptosis (IAP) repeat
Superfamily Superfamily superfamilyg.52.1 — Inhibitor of apoptosis (IAP) repeat
Family Family familyg.52.1.1 — Inhibitor of apoptosis (IAP) repeat
Domain ID domain_idd3uikb_
Class classg — Small proteins
Fold Fold foldg.52 — Inhibitor of apoptosis (IAP) repeat
Superfamily Superfamily superfamilyg.52.1 — Inhibitor of apoptosis (IAP) repeat
Family Family familyg.52.1.1 — Inhibitor of apoptosis (IAP) repeat

CATH v4.4 (2 domains)

Domain ID domain_id3uikA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1170 — Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A
Homologous superfamily homologous superfamily10 — Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A
Domain ID domain_id3uikB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1170 — Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A
Homologous superfamily homologous superfamily10 — Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A

8. Citations (1)

9. Files and Curves (10)