9z2n

CryoEM structure of human NSUN2(C271A) with SAH cross-linked to tRNA Lys(CTT) (D-arm conformation)

Method: ELECTRON MICROSCOPY Dmax: 91.6 Å Quality: GOOD

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

RNA cytosine C(5)-methyltransferase NSUN2

Homo sapiens

UniProt Q08J23

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 A; UniProt 2–767 Not recorded tRNA Lys(CTT) × 1 S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.57 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NSUN2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–782; UniProt 2–767

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 9z2n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9z2n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9z2n
Deposition date deposition_date2025-11-05
Structure title titleCryoEM structure of human NSUN2(C271A) with SAH cross-linked to tRNA Lys(CTT) (D-arm conformation)
Keywords keywordsTransferase, Methyltransferase, tRNA, Complex; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.10
Radius of gyration Rg (electron density) rg_electron28.34
Forward intensity I(0) i0325356000.00
Molecular weight molecular_weight87773.0 kDa
Excluded volume excluded_volume80174 ų
Envelope volume envelope_volume146180 ų
Hydration-shell volume shell_volume41760 ų
Envelope diameter envelope_diameter96.0
Shell Rg shell_rg36.72
Envelope Rg envelope_rg28.31
Shape Rg shape_rg28.30
Total Rg total_rg28.94
Total atoms total_atoms6481
Residues n_residues675
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 dmax91.6
Rg (real space) rg_real28.97
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real3.2540e+08
I(0) uncertainty (real space) i0_real_error4.6610e+06
Rg (reciprocal space) rg_reciprocal29.03
I(0) (reciprocal space) i0_reciprocal325400000.0000
Solution quality estimate total_estimate0.8970
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.6
Skewness Skewness skewness0.217
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25710000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)