1o0l

THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY

Method: SOLUTION NMR Dmax: 69.4 Å Quality: REASONABLE

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

Apoptosis regulator Bcl-W

Homo sapiens

UniProt Q92843

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–183 Mutation:A128E No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.7;303.15 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR measurement conditions:pH 6.7;303.15 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR measurement conditions:pH 6.7;303.15 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1 mM Bcl-w | 50mM Sodium Phosphate, 70mM NaCl, 2mM TCEP, 95% H2O, 5% D2O NMR sample composition:1 mM, U-15N Bcl-w | 50mM Sodium Phosphate, 70mM NaCl, 2mM TCEP, 95% H2O, 5% D2O NMR sample composition:1 mM, U-13C, 15N, Bcl-w | 50mM Sodium Phosphate, 70mM NaCl, 2mM TCEP, 95% H2O, 5% D2O 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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BCLW_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–188; UniProt 1–183

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 1o0l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1o0l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1o0l
Deposition date deposition_date2003-02-22
Structure title titleTHE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN MODULATING BIOLOGICAL ACTIVITY
Keywords keywordsAPOPTOSIS, BCL-2, HELICAL BUNDLE, BINDING GROOVE, BH3; APOPTOSIS
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.09
Radius of gyration Rg (electron density) rg_electron16.66
Forward intensity I(0) i02365540000.00
Molecular weight molecular_weight404600.0 kDa
Excluded volume excluded_volume502100 ų
Envelope volume envelope_volume66044 ų
Hydration-shell volume shell_volume23908 ų
Envelope diameter envelope_diameter80.7
Shell Rg shell_rg30.38
Envelope Rg envelope_rg25.70
Shape Rg shape_rg16.60
Total Rg total_rg17.12
Total atoms total_atoms56080
Residues n_residues3760
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 dmax69.4
Rg (real space) rg_real17.11
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real2.3660e+09
I(0) uncertainty (real space) i0_real_error2.9530e+07
Rg (reciprocal space) rg_reciprocal17.11
I(0) (reciprocal space) i0_reciprocal2366000000.0000
Solution quality estimate total_estimate0.7446
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.539
Kurtosis Kurtosis kurtosis0.657
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1189000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.311; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.742; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1o0la1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.1 — Toxins' membrane translocation domains
Superfamily Superfamily superfamilyf.1.4 — Bcl-2 inhibitors of programmed cell death
Family Family familyf.1.4.1 — Bcl-2 inhibitors of programmed cell death
Domain ID domain_idd1o0la2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1o0lA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology437 — Apoptosis Regulator Bcl-x
Homologous superfamily homologous superfamily10 — Blc2-like

8. Citations (1)

9. Files and Curves (10)