8ipi

The apo structure of human mitochondrial methyltransferase METTL15

Method: X-RAY DIFFRACTION Dmax: 67.5 Å Quality: GOOD

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

12S rRNA N4-methylcytidine (m4C) methyltransferase

Homo sapiens

UniProt A6NJ78

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 70–407 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;10% PEG MME 2000, 0.2M Ammonium sulfate, 0.1 M sodium acetate (pH 5.5) Resolution 2.10 Å R-free 0.229

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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET15_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–338; UniProt 70–407

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 8ipi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ipi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ipi
Deposition date deposition_date2023-03-14
Structure title titleThe apo structure of human mitochondrial methyltransferase METTL15
Keywords keywordshuman mitochondrial methyltransferase METTL15, RIBOSOMAL PROTEIN; RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.91
Radius of gyration Rg (electron density) rg_electron20.16
Forward intensity I(0) i018471800.00
Molecular weight molecular_weight32824.0 kDa
Excluded volume excluded_volume41290 ų
Envelope volume envelope_volume48857 ų
Hydration-shell volume shell_volume20574 ų
Envelope diameter envelope_diameter68.3
Shell Rg shell_rg26.37
Envelope Rg envelope_rg20.32
Shape Rg shape_rg20.17
Total Rg total_rg20.98
Total atoms total_atoms2307
Residues n_residues306
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 dmax67.5
Rg (real space) rg_real20.87
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.8470e+07
I(0) uncertainty (real space) i0_real_error2.3860e+05
Rg (reciprocal space) rg_reciprocal20.88
I(0) (reciprocal space) i0_reciprocal18470000.0000
Solution quality estimate total_estimate0.8887
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.331
Kurtosis Kurtosis kurtosis-0.284
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4071000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)