4nut

Crystal structure of the complex between Snu13p and the PEP domain of Rsa1

Method: X-RAY DIFFRACTION Dmax: 55.6 Å Quality: GOOD

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

13 kDa ribonucleoprotein-associated protein

Saccharomyces cerevisiae

UniProt P39990

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–126 Not recorded Ribosome assembly 1 protein × 1 (Q08932) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;293 K;2.3M ammonium sulfate, 70mM sodium citrate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.55 Å R-free 0.235

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.

47 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNU13_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–129; UniProt 1–126

Ribosome assembly 1 protein

Saccharomyces cerevisiae

UniProt Q08932

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 238–290 Fragment:PEP domain, UNP residues 238-290 13 kDa ribonucleoprotein-associated protein × 1 (P39990) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;293 K;2.3M ammonium sulfate, 70mM sodium citrate, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.55 Å R-free 0.235

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RSA1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–57; UniProt 238–290

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 4nut

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4nut
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4nut
Deposition date deposition_date2013-12-04
Structure title titleCrystal structure of the complex between Snu13p and the PEP domain of Rsa1
Keywords keywordsSnoRNP assembly, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.96
Radius of gyration Rg (electron density) rg_electron14.46
Forward intensity I(0) i05252310.00
Molecular weight molecular_weight16733.0 kDa
Excluded volume excluded_volume21173 ų
Envelope volume envelope_volume23428 ų
Hydration-shell volume shell_volume13565 ų
Envelope diameter envelope_diameter53.2
Shell Rg shell_rg20.51
Envelope Rg envelope_rg14.87
Shape Rg shape_rg14.43
Total Rg total_rg15.74
Total atoms total_atoms1172
Residues n_residues149
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 dmax55.6
Rg (real space) rg_real15.85
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real5.2520e+06
I(0) uncertainty (real space) i0_real_error5.3090e+04
Rg (reciprocal space) rg_reciprocal15.87
I(0) (reciprocal space) i0_reciprocal5252000.0000
Solution quality estimate total_estimate0.8428
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.143
Kurtosis Kurtosis kurtosis-0.260
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1384000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.653; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4nutA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1330 — 60s Ribosomal Protein L30; Chain: A;
Homologous superfamily homologous superfamily30 — Ribosomal protein L30/S12

8. Citations (1)

9. Files and Curves (10)