1xox

SOLUTION STRUCTURE OF HUMAN SURVIVIN

Method: SOLUTION NMR Dmax: 81.0 Å Quality: GOOD

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 1–117 Chain B; UniProt 1–117 Fragment:residues 1-117 ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 50 mM phosphate;Pressure ambient Resolution not provided

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 1–117; UniProt 1–117 Author chain B; PDBConstruct 1–117; UniProt 1–117

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 1xox

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xox
Deposition date deposition_date2004-10-07
Structure title titleSOLUTION STRUCTURE OF HUMAN SURVIVIN
Keywords keywordsBir Domain; Apoptosis, APOPTOSIS; APOPTOSIS
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier24.46
Radius of gyration Rg (electron density) rg_electron23.55
Forward intensity I(0) i013554000.00
Molecular weight molecular_weight27035.0 kDa
Excluded volume excluded_volume33625 ų
Envelope volume envelope_volume43523 ų
Hydration-shell volume shell_volume17261 ų
Envelope diameter envelope_diameter80.8
Shell Rg shell_rg27.84
Envelope Rg envelope_rg23.58
Shape Rg shape_rg23.54
Total Rg total_rg24.20
Total atoms total_atoms3708
Residues n_residues234
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 dmax81.0
Rg (real space) rg_real24.76
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.3550e+07
I(0) uncertainty (real space) i0_real_error2.0670e+05
Rg (reciprocal space) rg_reciprocal24.69
I(0) (reciprocal space) i0_reciprocal13550000.0000
Solution quality estimate total_estimate0.8181
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.6
Skewness Skewness skewness0.495
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2606000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.537; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1xoxa_
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_idd1xoxb_
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_id1xoxA00
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_id1xoxB00
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)