9g25

snR30 snoRNP - State 1 - Utp23-Krr1-deltaC3

Method: ELECTRON MICROSCOPY Dmax: 163.2 Å Quality: GOOD

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

H/ACA ribonucleoprotein complex subunit CBF5

OrganismNot specified

UniProt P33322

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain A; UniProt 1–483 Chain E; UniProt 1–483 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit NOP10 × 2 (Q6Q547) H/ACA ribonucleoprotein complex subunit GAR1 × 1 (P28007) H/ACA ribonucleoprotein complex subunit NHP2 × 2 (P32495) KRR1 small subunit processome component × 1 (P25586) Protein KRI1 × 1 (P42846) 40S ribosomal protein S13 × 1 (P05756) rRNA-processing protein UTP23 × 1 (Q12339) 40S ribosomal protein S14-A × 1 (P06367) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBF5_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–483; UniProt 1–483 Author chain E; PDBConstruct 1–483; UniProt 1–483

H/ACA ribonucleoprotein complex subunit NOP10

OrganismNot specified

UniProt Q6Q547

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain B; UniProt 1–58 Chain F; UniProt 1–58 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit CBF5 × 2 (P33322) H/ACA ribonucleoprotein complex subunit GAR1 × 1 (P28007) H/ACA ribonucleoprotein complex subunit NHP2 × 2 (P32495) KRR1 small subunit processome component × 1 (P25586) Protein KRI1 × 1 (P42846) 40S ribosomal protein S13 × 1 (P05756) rRNA-processing protein UTP23 × 1 (Q12339) 40S ribosomal protein S14-A × 1 (P06367) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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.

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

View Construct and Data Evidence
UniProt name NOP10_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–58; UniProt 1–58 Author chain F; PDBConstruct 1–58; UniProt 1–58

H/ACA ribonucleoprotein complex subunit GAR1

OrganismNot specified

UniProt P28007

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain C; UniProt 1–205 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit CBF5 × 2 (P33322) H/ACA ribonucleoprotein complex subunit NOP10 × 2 (Q6Q547) H/ACA ribonucleoprotein complex subunit NHP2 × 2 (P32495) KRR1 small subunit processome component × 1 (P25586) Protein KRI1 × 1 (P42846) 40S ribosomal protein S13 × 1 (P05756) rRNA-processing protein UTP23 × 1 (Q12339) 40S ribosomal protein S14-A × 1 (P06367) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GAR1_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–205; UniProt 1–205

H/ACA ribonucleoprotein complex subunit NHP2

OrganismNot specified

UniProt P32495

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain D; UniProt 1–156 Chain G; UniProt 1–156 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit CBF5 × 2 (P33322) H/ACA ribonucleoprotein complex subunit NOP10 × 2 (Q6Q547) H/ACA ribonucleoprotein complex subunit GAR1 × 1 (P28007) KRR1 small subunit processome component × 1 (P25586) Protein KRI1 × 1 (P42846) 40S ribosomal protein S13 × 1 (P05756) rRNA-processing protein UTP23 × 1 (Q12339) 40S ribosomal protein S14-A × 1 (P06367) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NHP2_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain D; PDBConstruct 1–156; UniProt 1–156 Author chain G; PDBConstruct 1–156; UniProt 1–156

KRR1 small subunit processome component

OrganismNot specified

UniProt P25586

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain H; UniProt 1–316 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit CBF5 × 2 (P33322) H/ACA ribonucleoprotein complex subunit NOP10 × 2 (Q6Q547) H/ACA ribonucleoprotein complex subunit GAR1 × 1 (P28007) H/ACA ribonucleoprotein complex subunit NHP2 × 2 (P32495) Protein KRI1 × 1 (P42846) 40S ribosomal protein S13 × 1 (P05756) rRNA-processing protein UTP23 × 1 (Q12339) 40S ribosomal protein S14-A × 1 (P06367) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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.

20 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KRR1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain H; PDBConstruct 1–316; UniProt 1–316

Protein KRI1

OrganismNot specified

UniProt P42846

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain I; UniProt 1–591 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit CBF5 × 2 (P33322) H/ACA ribonucleoprotein complex subunit NOP10 × 2 (Q6Q547) H/ACA ribonucleoprotein complex subunit GAR1 × 1 (P28007) H/ACA ribonucleoprotein complex subunit NHP2 × 2 (P32495) KRR1 small subunit processome component × 1 (P25586) 40S ribosomal protein S13 × 1 (P05756) rRNA-processing protein UTP23 × 1 (Q12339) 40S ribosomal protein S14-A × 1 (P06367) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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 KRI1_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain I; PDBConstruct 1–591; UniProt 1–591

40S ribosomal protein S13

OrganismNot specified

UniProt P05756

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain J; UniProt 1–151 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit CBF5 × 2 (P33322) H/ACA ribonucleoprotein complex subunit NOP10 × 2 (Q6Q547) H/ACA ribonucleoprotein complex subunit GAR1 × 1 (P28007) H/ACA ribonucleoprotein complex subunit NHP2 × 2 (P32495) KRR1 small subunit processome component × 1 (P25586) Protein KRI1 × 1 (P42846) rRNA-processing protein UTP23 × 1 (Q12339) 40S ribosomal protein S14-A × 1 (P06367) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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.

204 other PDB entries and 243 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS13_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain J; PDBConstruct 1–151; UniProt 1–151

rRNA-processing protein UTP23

OrganismNot specified

UniProt Q12339

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain K; UniProt 1–254 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit CBF5 × 2 (P33322) H/ACA ribonucleoprotein complex subunit NOP10 × 2 (Q6Q547) H/ACA ribonucleoprotein complex subunit GAR1 × 1 (P28007) H/ACA ribonucleoprotein complex subunit NHP2 × 2 (P32495) KRR1 small subunit processome component × 1 (P25586) Protein KRI1 × 1 (P42846) 40S ribosomal protein S13 × 1 (P05756) 40S ribosomal protein S14-A × 1 (P06367) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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 UTP23_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain K; PDBConstruct 1–254; UniProt 1–254

40S ribosomal protein S14-A

OrganismNot specified

UniProt P06367

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–RNA Heteromer Protein × 12 RNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain L; UniProt 1–137 Not recorded RDN18-1 × 1 snR30 × 1 H/ACA ribonucleoprotein complex subunit CBF5 × 2 (P33322) H/ACA ribonucleoprotein complex subunit NOP10 × 2 (Q6Q547) H/ACA ribonucleoprotein complex subunit GAR1 × 1 (P28007) H/ACA ribonucleoprotein complex subunit NHP2 × 2 (P32495) KRR1 small subunit processome component × 1 (P25586) Protein KRI1 × 1 (P42846) 40S ribosomal protein S13 × 1 (P05756) rRNA-processing protein UTP23 × 1 (Q12339) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 Å

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.

153 other PDB entries and 180 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS14A_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain L; PDBConstruct 1–137; UniProt 1–137

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 9g25

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9g25
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9g25
Deposition date deposition_date2024-07-10
最后修订 last_revision2025-06-18
Structure title titlesnR30 snoRNP - State 1 - Utp23-Krr1-deltaC3
Keywords keywords90S, pre-ribosome, snoRNA, snR30, snoRNP, ribosome biogenesis, H/ACA, 18S rRNA, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.58
Radius of gyration Rg (electron density) rg_electron52.80
Forward intensity I(0) i02709200000.00
Molecular weight molecular_weight348910.0 kDa
Excluded volume excluded_volume400520 ų
Envelope volume envelope_volume651000 ų
Hydration-shell volume shell_volume100650 ų
Envelope diameter envelope_diameter171.9
Shell Rg shell_rg58.87
Envelope Rg envelope_rg50.69
Shape Rg shape_rg52.80
Total Rg total_rg52.95
Total atoms total_atoms24015
Residues n_residues2463
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 dmax163.2
Rg (real space) rg_real53.28
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real2.7090e+09
I(0) uncertainty (real space) i0_real_error5.3640e+07
Rg (reciprocal space) rg_reciprocal53.81
I(0) (reciprocal space) i0_reciprocal2711000000.0000
Solution quality estimate total_estimate0.8833
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary78.8
Skewness Skewness skewness-0.045
Kurtosis Kurtosis kurtosis-0.653
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha131500000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.719

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (2)

9. Files and Curves (10)