1e31

SURVIVIN DIMER H. SAPIENS

Method: X-RAY DIFFRACTION Dmax: 108.8 Å Quality: REASONABLE

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

APOPTOSIS INHIBITOR SURVIVIN

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–142 Chain B; UniProt 1–142 Not recorded ZN ZINC ION × 2 CO COBALT (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;3 % PEG MME 2K, 2 MM HEXAMINE COBALT, 100 MM HEPES PH 7.1 Resolution 2.71 Å R-free 0.270

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 IAP4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–142; UniProt 1–142 Author chain B; PDBConstruct 1–142; 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 1e31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1e31
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1e31
Deposition date deposition_date2000-06-04
Structure title titleSURVIVIN DIMER H. SAPIENS
Keywords keywordsAPOPTOSIS INHIBITOR, IAP, APOTOSIS, ZINC FINGER; APOPTOSIS INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.82
Radius of gyration Rg (electron density) rg_electron28.39
Forward intensity I(0) i017924700.00
Molecular weight molecular_weight31923.0 kDa
Excluded volume excluded_volume39748 ų
Envelope volume envelope_volume55060 ų
Hydration-shell volume shell_volume18430 ų
Envelope diameter envelope_diameter113.8
Shell Rg shell_rg31.02
Envelope Rg envelope_rg29.19
Shape Rg shape_rg28.33
Total Rg total_rg28.87
Total atoms total_atoms2236
Residues n_residues274
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 dmax108.8
Rg (real space) rg_real29.13
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real1.7920e+07
I(0) uncertainty (real space) i0_real_error3.1020e+05
Rg (reciprocal space) rg_reciprocal29.00
I(0) (reciprocal space) i0_reciprocal17920000.0000
Solution quality estimate total_estimate0.7302
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.489
Kurtosis Kurtosis kurtosis-0.423
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1997000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.461; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.147; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1e31a_
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_idd1e31b_
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_id1e31A00
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_id1e31B00
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)