9xzq

Trm10-tRNA complex (closed conformation)

Method: ELECTRON MICROSCOPY Dmax: 82.2 Å Quality: GOOD

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

tRNA (guanine(9)-N1)-methyltransferase

Saccharomyces cerevisiae

UniProt Q12400

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 Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain B; UniProt 1–293 Not recorded Transfer RNA (Gly) × 1 AN6 5'-{[(3S)-3-amino-3-carboxypropyl](ethyl)amino}-5'-deoxyadenosine × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.63 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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRM10_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–293; UniProt 1–293

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 9xzq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9xzq
Deposition date deposition_date2025-08-27
Structure title titleTrm10-tRNA complex (closed conformation)
Keywords keywordsSPOUT methyltransferase, Complex, tRNA, methylation, RNA BINDING PROTEIN, RNA BINDING PROTEIN-RNA complex; RNA BINDING PROTEIN/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier24.70
Radius of gyration Rg (electron density) rg_electron23.48
Forward intensity I(0) i063613900.00
Molecular weight molecular_weight45363.0 kDa
Excluded volume excluded_volume49493 ų
Envelope volume envelope_volume69870 ų
Hydration-shell volume shell_volume25682 ų
Envelope diameter envelope_diameter86.2
Shell Rg shell_rg29.76
Envelope Rg envelope_rg23.11
Shape Rg shape_rg23.40
Total Rg total_rg24.20
Total atoms total_atoms3090
Residues n_residues259
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 dmax82.2
Rg (real space) rg_real24.64
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real6.3610e+07
I(0) uncertainty (real space) i0_real_error9.1320e+05
Rg (reciprocal space) rg_reciprocal24.66
I(0) (reciprocal space) i0_reciprocal63610000.0000
Solution quality estimate total_estimate0.8112
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary31.3
Skewness Skewness skewness0.279
Kurtosis Kurtosis kurtosis-0.354
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4586000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)