7d8d

The crystal structure of ScNTM1 in complex with SAH and Rps25a hexapeptide

Method: X-RAY DIFFRACTION Dmax: 58.4 Å Quality: GOOD

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

Alpha N-terminal protein methyltransferase 1

Saccharomyces cerevisiae

UniProt P38340

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 1–232 Not recorded Rps25A-peptide × 1 (Q3E792) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.2M magnesium chloride hexahydrate,0.1M Bis-Tris(pH 6.5) and 25% PEG3350 Resolution 1.05 Å R-free 0.136

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NTM1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–232; UniProt 1–232

Rps25A-peptide

OrganismNot specified

UniProt Q3E792

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 D; UniProt 2–7 Not recorded Alpha N-terminal protein methyltransferase 1 × 1 (P38340) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.2M magnesium chloride hexahydrate,0.1M Bis-Tris(pH 6.5) and 25% PEG3350 Resolution 1.05 Å R-free 0.136

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.

130 other PDB entries and 169 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS25A_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–6; UniProt 2–7

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 7d8d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7d8d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7d8d
Deposition date deposition_date2020-10-08
Structure title titleThe crystal structure of ScNTM1 in complex with SAH and Rps25a hexapeptide
Keywords keywordsScNTM1; N-terminal methylation; methyltransferase; Saccharomyces cerevisiae; substrate binding pocket, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.01
Radius of gyration Rg (electron density) rg_electron16.68
Forward intensity I(0) i013117100.00
Molecular weight molecular_weight27120.0 kDa
Excluded volume excluded_volume33951 ų
Envelope volume envelope_volume37837 ų
Hydration-shell volume shell_volume18396 ų
Envelope diameter envelope_diameter59.1
Shell Rg shell_rg23.50
Envelope Rg envelope_rg17.10
Shape Rg shape_rg16.67
Total Rg total_rg17.76
Total atoms total_atoms3792
Residues n_residues238
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 dmax58.4
Rg (real space) rg_real17.86
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real1.3120e+07
I(0) uncertainty (real space) i0_real_error1.4070e+05
Rg (reciprocal space) rg_reciprocal17.88
I(0) (reciprocal space) i0_reciprocal13120000.0000
Solution quality estimate total_estimate0.8764
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.124
Kurtosis Kurtosis kurtosis-0.361
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5732000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)