7lms

Structure of human SetD3 methyl-transferase in complex with 2A protease from Coxsackievirus B3

Method: ELECTRON MICROSCOPY Dmax: 85.3 Å Quality: EXCELLENT

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

Protease 2A

Coxsackievirus B3 (strain Nancy)

UniProt P03313

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 B; UniProt 855–1001 Mutation:C107A Actin-histidine N-methyltransferase × 1 (Q86TU7) ZN ZINC ION × 1 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

20 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_CXB3N
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 5–151; UniProt 855–1001

Actin-histidine N-methyltransferase

Homo sapiens

UniProt Q86TU7

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 2–594 Not recorded Protease 2A × 1 (P03313) ZN ZINC ION × 1 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

21 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SETD3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 4–596; UniProt 2–594

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 7lms

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7lms
Deposition date deposition_date2021-02-05
Structure title titleStructure of human SetD3 methyl-transferase in complex with 2A protease from Coxsackievirus B3
Keywords keywordsMethyltransferase, viral protease, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier27.51
Radius of gyration Rg (electron density) rg_electron26.42
Forward intensity I(0) i080481700.00
Molecular weight molecular_weight70225.0 kDa
Excluded volume excluded_volume87871 ų
Envelope volume envelope_volume109190 ų
Hydration-shell volume shell_volume33885 ų
Envelope diameter envelope_diameter90.5
Shell Rg shell_rg34.21
Envelope Rg envelope_rg26.25
Shape Rg shape_rg26.42
Total Rg total_rg27.26
Total atoms total_atoms4947
Residues n_residues612
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 dmax85.3
Rg (real space) rg_real27.36
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real8.0480e+07
I(0) uncertainty (real space) i0_real_error1.1290e+06
Rg (reciprocal space) rg_reciprocal27.41
I(0) (reciprocal space) i0_reciprocal80480000.0000
Solution quality estimate total_estimate0.9081
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.161
Kurtosis Kurtosis kurtosis-0.505
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17900000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)