6w89

Structure of DNMT3A (R882H) in complex with CGA DNA

Method: X-RAY DIFFRACTION Dmax: 190.1 Å Quality: GOOD

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

DNA (cytosine-5)-methyltransferase 3A

Homo sapiens

UniProt Q9Y6K1

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 628–912 Chain D; UniProt 628–912 Not recorded DNA (cytosine-5)-methyltransferase 3-like × 2 (Q9UJW3) CGA DNA (25-MER) × 2 CIT CITRIC ACID × 2 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1 M Sodium Citrate pH 4.2, 1% PEG8000 Resolution 2.50 Å R-free 0.240
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain G; UniProt 628–912 Chain J; UniProt 628–912 Not recorded DNA (cytosine-5)-methyltransferase 3-like × 2 (Q9UJW3) CGA DNA (25-MER) × 2 CIT CITRIC ACID × 2 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1 M Sodium Citrate pH 4.2, 1% PEG8000 Resolution 2.50 Å R-free 0.240

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.

42 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNM3A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–285; UniProt 628–912 Author chain D; PDBConstruct 1–285; UniProt 628–912 Author chain G; PDBConstruct 1–285; UniProt 628–912 Author chain J; PDBConstruct 1–285; UniProt 628–912

DNA (cytosine-5)-methyltransferase 3-like

Homo sapiens

UniProt Q9UJW3

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 178–386 Chain C; UniProt 178–386 Not recorded DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) CGA DNA (25-MER) × 2 CIT CITRIC ACID × 2 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1 M Sodium Citrate pH 4.2, 1% PEG8000 Resolution 2.50 Å R-free 0.240
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain H; UniProt 178–386 Chain I; UniProt 178–386 Not recorded DNA (cytosine-5)-methyltransferase 3A × 2 (Q9Y6K1) CGA DNA (25-MER) × 2 CIT CITRIC ACID × 2 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1 M Sodium Citrate pH 4.2, 1% PEG8000 Resolution 2.50 Å R-free 0.240

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.

28 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNM3L_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–209; UniProt 178–386 Author chain C; PDBConstruct 1–209; UniProt 178–386 Author chain H; PDBConstruct 1–209; UniProt 178–386 Author chain I; PDBConstruct 1–209; UniProt 178–386

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 6w89

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6w89
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6w89
Deposition date deposition_date2020-03-20
Structure title titleStructure of DNMT3A (R882H) in complex with CGA DNA
Keywords keywordsDNA methylation, DNMT3A(R882H), AML, epigenetics, TRANSFERASE, TRANSFERASE-DNA complex; TRANSFERASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier49.75
Radius of gyration Rg (electron density) rg_electron50.86
Forward intensity I(0) i0967924000.00
Molecular weight molecular_weight239390.0 kDa
Excluded volume excluded_volume291260 ų
Envelope volume envelope_volume417870 ų
Hydration-shell volume shell_volume72533 ų
Envelope diameter envelope_diameter206.8
Shell Rg shell_rg50.18
Envelope Rg envelope_rg51.70
Shape Rg shape_rg50.97
Total Rg total_rg50.48
Total atoms total_atoms16786
Residues n_residues1984
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 dmax190.1
Rg (real space) rg_real50.42
Rg uncertainty (real space) rg_real_error2.48
I(0) (real space) i0_real9.6790e+08
I(0) uncertainty (real space) i0_real_error2.0470e+07
Rg (reciprocal space) rg_reciprocal49.75
I(0) (reciprocal space) i0_reciprocal967100000.0000
Solution quality estimate total_estimate0.8051
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.5
Skewness Skewness skewness0.663
Kurtosis Kurtosis kurtosis0.220
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55400000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.585; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.794; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6w89B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id6w89C00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id6w89H00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39
Domain ID domain_id6w89I00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily150 — Vaccinia Virus protein VP39

8. Citations (1)

9. Files and Curves (10)