6kms

Crystal structure of human N6amt1-Trm112 in complex with SAM (space group I422)

Method: X-RAY DIFFRACTION Dmax: 95.2 Å Quality: GOOD

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

Methyltransferase N6AMT1

Homo sapiens

UniProt Q9Y5N5

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–214 Non-standard monomer:Yes (specific site not provided by mmCIF) Multifunctional methyltransferase subunit TRM112-like protein × 1 (Q9UI30) SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;1.6M (NH4)2SO4, 0.1M MES, pH 6.5, 10% 1,4-Dioxane Resolution 3.20 Å R-free 0.269
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–214 Non-standard monomer:Yes (specific site not provided by mmCIF) Multifunctional methyltransferase subunit TRM112-like protein × 1 (Q9UI30) SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;1.6M (NH4)2SO4, 0.1M MES, pH 6.5, 10% 1,4-Dioxane Resolution 3.20 Å R-free 0.269

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name N6MT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 15–228; UniProt 1–214 Author chain D; PDBConstruct 15–228; UniProt 1–214

Multifunctional methyltransferase subunit TRM112-like protein

Homo sapiens

UniProt Q9UI30

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–125 Non-standard monomer:Yes (specific site not provided by mmCIF) Methyltransferase N6AMT1 × 1 (Q9Y5N5) SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;1.6M (NH4)2SO4, 0.1M MES, pH 6.5, 10% 1,4-Dioxane Resolution 3.20 Å R-free 0.269
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–125 Non-standard monomer:Yes (specific site not provided by mmCIF) Methyltransferase N6AMT1 × 1 (Q9Y5N5) SAM S-ADENOSYLMETHIONINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;1.6M (NH4)2SO4, 0.1M MES, pH 6.5, 10% 1,4-Dioxane Resolution 3.20 Å R-free 0.269

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.

26 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TR112_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 2–126; UniProt 1–125 Author chain B; PDBConstruct 2–126; UniProt 1–125

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 6kms

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6kms
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6kms
Deposition date deposition_date2019-08-01
Structure title titleCrystal structure of human N6amt1-Trm112 in complex with SAM (space group I422)
Keywords keywordsmethyltransferase, complex, protein translation, polypeptide release factor eRF1, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.24
Radius of gyration Rg (electron density) rg_electron29.71
Forward intensity I(0) i087921800.00
Molecular weight molecular_weight73504.0 kDa
Excluded volume excluded_volume91491 ų
Envelope volume envelope_volume113040 ų
Hydration-shell volume shell_volume32149 ų
Envelope diameter envelope_diameter98.8
Shell Rg shell_rg36.32
Envelope Rg envelope_rg29.67
Shape Rg shape_rg29.75
Total Rg total_rg30.19
Total atoms total_atoms5097
Residues n_residues645
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 dmax95.2
Rg (real space) rg_real30.30
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real8.7920e+07
I(0) uncertainty (real space) i0_real_error1.4450e+06
Rg (reciprocal space) rg_reciprocal30.28
I(0) (reciprocal space) i0_reciprocal87920000.0000
Solution quality estimate total_estimate0.8883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.331
Kurtosis Kurtosis kurtosis-0.624
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19500000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.827

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)