9z2p

CryoEM structure of human NSUN2 with tRNA Lys(CTT) (Conformation 1)

Method: ELECTRON MICROSCOPY Dmax: 90.2 Å Quality: EXCELLENT

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 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 2.91 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 9z2p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9z2p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9z2p
Deposition date deposition_date2025-11-05
Structure title titleCryoEM structure of human NSUN2 with tRNA Lys(CTT) (Conformation 1)
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_guinier29.84
Radius of gyration Rg (electron density) rg_electron28.78
Forward intensity I(0) i0188998000.00
Molecular weight molecular_weight92397.0 kDa
Excluded volume excluded_volume108500 ų
Envelope volume envelope_volume148100 ų
Hydration-shell volume shell_volume41895 ų
Envelope diameter envelope_diameter96.0
Shell Rg shell_rg37.10
Envelope Rg envelope_rg28.65
Shape Rg shape_rg28.77
Total Rg total_rg29.48
Total atoms total_atoms6390
Residues n_residues667
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 dmax90.2
Rg (real space) rg_real29.69
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.8900e+08
I(0) uncertainty (real space) i0_real_error2.6960e+06
Rg (reciprocal space) rg_reciprocal29.76
I(0) (reciprocal space) i0_reciprocal189000000.0000
Solution quality estimate total_estimate0.9038
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.5
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16870000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)