5wxm

Crystal structure of the Imp3 and Mpp10 complex

Method: X-RAY DIFFRACTION Dmax: 69.2 Å Quality: GOOD

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

U3 small nucleolar ribonucleoprotein protein IMP3

Saccharomyces cerevisiae S288c

UniProt P32899

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 26–183 Chain B; UniProt 26–183 Fragment:UNP residues 26-183 Non-standard monomer:Yes (specific site not provided by mmCIF) U3 small nucleolar RNA-associated protein MPP10 × 2 (P47083) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;0.2 M potassium sodium tartrate, 0.1 M sodium citrate, 1.7 M ammonium sulfate Resolution 2.30 Å R-free 0.237

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.

38 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMP3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–159; UniProt 26–183 Author chain B; PDBConstruct 2–159; UniProt 26–183

U3 small nucleolar RNA-associated protein MPP10

Saccharomyces cerevisiae S288c

UniProt P47083

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain U; UniProt 430–461 Chain V; UniProt 430–461 Fragment:UNP residues 430-461 U3 small nucleolar ribonucleoprotein protein IMP3 × 2 (P32899) SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;0.2 M potassium sodium tartrate, 0.1 M sodium citrate, 1.7 M ammonium sulfate Resolution 2.30 Å R-free 0.237

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.

44 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MPP10_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain U; PDBConstruct 3–34; UniProt 430–461 Author chain V; PDBConstruct 3–34; UniProt 430–461

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 5wxm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wxm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5wxm
Deposition date deposition_date2017-01-07
Structure title titleCrystal structure of the Imp3 and Mpp10 complex
Keywords keywordsprotein complex, components of 90S preribosome, 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_guinier21.98
Radius of gyration Rg (electron density) rg_electron20.85
Forward intensity I(0) i027902400.00
Molecular weight molecular_weight39187.0 kDa
Excluded volume excluded_volume48561 ų
Envelope volume envelope_volume58637 ų
Hydration-shell volume shell_volume23328 ų
Envelope diameter envelope_diameter71.6
Shell Rg shell_rg27.45
Envelope Rg envelope_rg20.97
Shape Rg shape_rg20.86
Total Rg total_rg21.66
Total atoms total_atoms2711
Residues n_residues318
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 dmax69.2
Rg (real space) rg_real21.81
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.7900e+07
I(0) uncertainty (real space) i0_real_error3.3460e+05
Rg (reciprocal space) rg_reciprocal21.84
I(0) (reciprocal space) i0_reciprocal27900000.0000
Solution quality estimate total_estimate0.8996
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.092
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6644000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)