1a32

RIBOSOMAL PROTEIN S15 FROM BACILLUS STEAROTHERMOPHILUS

Method: X-RAY DIFFRACTION Dmax: 63.6 Å Quality: GOOD

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

RIBOSOMAL PROTEIN S15

Geobacillus stearothermophilus

UniProt P05766

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 1–88 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;3.0M NA/K PHOSPHATE PH 6.5 Resolution 2.10 Å R-free 0.318

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS15_BACST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–88; UniProt 1–88

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 1a32

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a32
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a32
Deposition date deposition_date1998-01-27
Structure title titleRIBOSOMAL PROTEIN S15 FROM BACILLUS STEAROTHERMOPHILUS
Keywords keywordsMULTIWAVELENGTH ANOMALOUS DIFFRACTION, PROTEIN-RNA, RIBOSOMAL PROTEIN INTERACTIONS, RIBOSOME, RNA-BINDING, RIBOSOMAL PROTEIN; RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.70
Radius of gyration Rg (electron density) rg_electron18.28
Forward intensity I(0) i02206220.00
Molecular weight molecular_weight10167.0 kDa
Excluded volume excluded_volume12719 ų
Envelope volume envelope_volume16960 ų
Hydration-shell volume shell_volume9119 ų
Envelope diameter envelope_diameter64.4
Shell Rg shell_rg21.58
Envelope Rg envelope_rg18.55
Shape Rg shape_rg18.27
Total Rg total_rg18.97
Total atoms total_atoms716
Residues n_residues85
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 dmax63.6
Rg (real space) rg_real18.82
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real2.2060e+06
I(0) uncertainty (real space) i0_real_error2.5320e+04
Rg (reciprocal space) rg_reciprocal18.80
I(0) (reciprocal space) i0_reciprocal2206000.0000
Solution quality estimate total_estimate0.8515
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary16.5
Skewness Skewness skewness0.322
Kurtosis Kurtosis kurtosis-0.651
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha179100.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.822; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.666; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a32a_
Class classa — All alpha proteins
Fold Fold folda.16 — S15/NS1 RNA-binding domain
Superfamily Superfamily superfamilya.16.1 — S15/NS1 RNA-binding domain
Family Family familya.16.1.2 — Ribosomal protein S15

CATH v4.4 (1 domains)

Domain ID domain_id1a32A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily10 — S15/NS1, RNA-binding

8. Citations (1)

9. Files and Curves (10)