6ox2

SETD3in Complex with an Actin Peptide with the Target Histidine Fully Methylated

Method: X-RAY DIFFRACTION Dmax: 119.2 Å Quality: GOOD

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

Actin Peptide

OrganismNot specified

UniProt P60709

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 Y; UniProt 66–80 Fragment:residues 66-80 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-lysine N-methyltransferase setd3 × 1 (Q86TU7) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000 Resolution 2.09 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Z; UniProt 66–80 Fragment:residues 66-80 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone-lysine N-methyltransferase setd3 × 1 (Q86TU7) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 8 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000 Resolution 2.09 Å R-free 0.239

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.

72 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain Y; PDBConstruct 1–15; UniProt 66–80 Author chain Z; PDBConstruct 1–15; UniProt 66–80

Histone-lysine N-methyltransferase setd3

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 1–594 Not recorded Actin Peptide × 1 (P60709) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000 Resolution 2.09 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–594 Not recorded Actin Peptide × 1 (P60709) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 8 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.6 and 30% (w/v) polyethylene glycol 4000 Resolution 2.09 Å R-free 0.239

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 41 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 6–599; UniProt 1–594 Author chain B; PDBConstruct 6–599; UniProt 1–594

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 6ox2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ox2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6ox2
Deposition date deposition_date2019-05-13
Structure title titleSETD3in Complex with an Actin Peptide with the Target Histidine Fully Methylated
Keywords keywordsTRANSFERASE, TRANSFERASE-STRUCTURAL PROTEIN complex; TRANSFERASE/STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.78
Radius of gyration Rg (electron density) rg_electron34.54
Forward intensity I(0) i0201782000.00
Molecular weight molecular_weight115650.0 kDa
Excluded volume excluded_volume145300 ų
Envelope volume envelope_volume184470 ų
Hydration-shell volume shell_volume45587 ų
Envelope diameter envelope_diameter127.5
Shell Rg shell_rg39.76
Envelope Rg envelope_rg34.91
Shape Rg shape_rg34.51
Total Rg total_rg35.03
Total atoms total_atoms8154
Residues n_residues994
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 dmax119.2
Rg (real space) rg_real34.88
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real2.0180e+08
I(0) uncertainty (real space) i0_real_error3.8780e+06
Rg (reciprocal space) rg_reciprocal34.82
I(0) (reciprocal space) i0_reciprocal201800000.0000
Solution quality estimate total_estimate0.8646
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.5
Skewness Skewness skewness0.479
Kurtosis Kurtosis kurtosis-0.124
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38910000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)