6mbl

SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, Second P212121 Crystal Form

Method: X-RAY DIFFRACTION Dmax: 83.4 Å Quality: EXCELLENT

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 Histone-lysine N-methyltransferase setd3 × 1 (Q86TU7) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 EDO 1,2-ETHANEDIOL × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;292 K;0.2 M Sodium chloride, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350 Resolution 2.20 Å R-free 0.227

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 83 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

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 × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;292 K;0.2 M Sodium chloride, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350 Resolution 2.20 Å R-free 0.227

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 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 6mbl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mbl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mbl
Deposition date deposition_date2018-08-30
Structure title titleSETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, Second P212121 Crystal Form
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_guinier26.69
Radius of gyration Rg (electron density) rg_electron25.84
Forward intensity I(0) i052870500.00
Molecular weight molecular_weight57591.0 kDa
Excluded volume excluded_volume72397 ų
Envelope volume envelope_volume88345 ų
Hydration-shell volume shell_volume28645 ų
Envelope diameter envelope_diameter86.4
Shell Rg shell_rg32.86
Envelope Rg envelope_rg25.93
Shape Rg shape_rg25.81
Total Rg total_rg26.66
Total atoms total_atoms4060
Residues n_residues496
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 dmax83.4
Rg (real space) rg_real26.67
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real5.2870e+07
I(0) uncertainty (real space) i0_real_error7.1530e+05
Rg (reciprocal space) rg_reciprocal26.68
I(0) (reciprocal space) i0_reciprocal52870000.0000
Solution quality estimate total_estimate0.9074
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.521
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13870000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6mblA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1410 — set domain protein methyltransferase, domain 1
Homologous superfamily homologous superfamily10 — set domain protein methyltransferase, domain 1
Domain ID domain_id6mblA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1420 — set domain protein methyltransferase, domain 2
Homologous superfamily homologous superfamily10 — Rubisco LSMT, substrate-binding domain

8. Citations (1)

9. Files and Curves (10)