9yfo

insect H/ACA snoRNP class IV

Method: ELECTRON MICROSCOPY Dmax: 128.5 Å Quality: EXCELLENT

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

H/ACA ribonucleoprotein complex subunit 4-like

OrganismNot specified

UniProt A0A7E5VBG0

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 × 7 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 1–514 Chain D; UniProt 1–514 Not recorded H/ACA ribonucleoprotein complex subunit × 1 (A0A7E5WAP8) H/ACA ribonucleoprotein complex subunit 2-like protein × 2 (A0A7E5W3Q7) H/ACA ribonucleoprotein complex subunit 3 × 2 (A0A7E5W2Q0) RNA (97-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 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 A0A7E5VBG0_TRINI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–514; UniProt 1–514 Author chain D; PDBConstruct 1–514; UniProt 1–514

H/ACA ribonucleoprotein complex subunit

OrganismNot specified

UniProt A0A7E5WAP8

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 × 7 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain B; UniProt 1–233 Not recorded H/ACA ribonucleoprotein complex subunit 4-like × 2 (A0A7E5VBG0) H/ACA ribonucleoprotein complex subunit 2-like protein × 2 (A0A7E5W3Q7) H/ACA ribonucleoprotein complex subunit 3 × 2 (A0A7E5W2Q0) RNA (97-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 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 A0A7E5WAP8_TRINI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–233; UniProt 1–233

H/ACA ribonucleoprotein complex subunit 2-like protein

OrganismNot specified

UniProt A0A7E5W3Q7

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 × 7 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain C; UniProt 1–156 Chain G; UniProt 1–156 Not recorded H/ACA ribonucleoprotein complex subunit 4-like × 2 (A0A7E5VBG0) H/ACA ribonucleoprotein complex subunit × 1 (A0A7E5WAP8) H/ACA ribonucleoprotein complex subunit 3 × 2 (A0A7E5W2Q0) RNA (97-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 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 A0A7E5W3Q7_TRINI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–156; UniProt 1–156 Author chain G; PDBConstruct 1–156; UniProt 1–156

H/ACA ribonucleoprotein complex subunit 3

OrganismNot specified

UniProt A0A7E5W2Q0

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 × 7 RNA 1 PDB declaration: octameric(8) Consistent with all polymer counts Chain F; UniProt 1–64 Chain H; UniProt 1–64 Not recorded H/ACA ribonucleoprotein complex subunit 4-like × 2 (A0A7E5VBG0) H/ACA ribonucleoprotein complex subunit × 1 (A0A7E5WAP8) H/ACA ribonucleoprotein complex subunit 2-like protein × 2 (A0A7E5W3Q7) RNA (97-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 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 A0A7E5W2Q0_TRINI
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–64; UniProt 1–64 Author chain H; PDBConstruct 1–64; UniProt 1–64

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 9yfo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9yfo
Deposition date deposition_date2025-09-26
Structure title titleinsect H/ACA snoRNP class IV
Keywords keywordsPseudouridine synthase, enzyme complex, snoRNA, snoRNP, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.84
Radius of gyration Rg (electron density) rg_electron38.48
Forward intensity I(0) i0501388000.00
Molecular weight molecular_weight163410.0 kDa
Excluded volume excluded_volume196520 ų
Envelope volume envelope_volume272180 ų
Hydration-shell volume shell_volume57963 ų
Envelope diameter envelope_diameter131.3
Shell Rg shell_rg45.42
Envelope Rg envelope_rg37.72
Shape Rg shape_rg38.42
Total Rg total_rg39.02
Total atoms total_atoms21932
Residues n_residues1264
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 dmax128.5
Rg (real space) rg_real39.65
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real5.0140e+08
I(0) uncertainty (real space) i0_real_error7.7140e+06
Rg (reciprocal space) rg_reciprocal39.77
I(0) (reciprocal space) i0_reciprocal501400000.0000
Solution quality estimate total_estimate0.9004
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.151
Kurtosis Kurtosis kurtosis-0.544
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31920000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.929

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)