DNA (cytosine-5)-methyltransferase 3A
Homo sapiens
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.
| Other PDB | Difference from Current Entry 6W89 | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 2QRV Structure of Dnmt3a-Dnmt3L C-terminal domain complex Deposited 2007-07-29 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain A
624–909(286 aa)
Fragment:residues 623 to 908
Chain D
624–909(286 aa)
Fragment:residues 623 to 908
|
Not recorded | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8;300 K;The final protein solution CONTAINED ~100 TO 133 micro M COMPLEX IN 20 milli M TRIS/HCL, PH 8.0, 100 milli M NACL, 5 % GLYCEROL, AND 0.1 % MERCAPTOETHANOL. Crystals were obtained with the mother liquor containing 2~5 % PEG 3000, 100 mM Tris/HCl, pH 8.0, 5 % glycerol at 16C, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.89 Å R-free 0.281 |
| 2QRV Structure of Dnmt3a-Dnmt3L C-terminal domain complex Deposited 2007-07-29 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain E
624–909(286 aa)
Fragment:residues 623 to 908
Chain H
624–909(286 aa)
Fragment:residues 623 to 908
|
Not recorded | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8;300 K;The final protein solution CONTAINED ~100 TO 133 micro M COMPLEX IN 20 milli M TRIS/HCL, PH 8.0, 100 milli M NACL, 5 % GLYCEROL, AND 0.1 % MERCAPTOETHANOL. Crystals were obtained with the mother liquor containing 2~5 % PEG 3000, 100 mM Tris/HCl, pH 8.0, 5 % glycerol at 16C, VAPOR DIFFUSION, HANGING DROP
|
Resolution 2.89 Å R-free 0.281 |
| 3A1A Crystal Structure of the DNMT3A ADD domain Deposited 2009-03-28 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
476–614(139 aa)
Fragment:ADD(ATRX-DNMT3-DNMT3L) domain, residues 476-614
|
Not recorded | ZN ZINC ION × 3 EDO 1,2-ETHANEDIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;17% PEG 8000, 0.1M Tris-HCl, 0.2M magnesium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.30 Å R-free 0.250 |
| 3A1B Crystal structure of the DNMT3A ADD domain in complex with histone H3 Deposited 2009-03-28 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
476–614(139 aa)
Fragment:ADD(ATRX-DNMT3-DNMT3L) domain(residues 476-614), UNP residues 2-21(Histone H3.1)
|
Not recorded | ZN ZINC ION × 3 EDO 1,2-ETHANEDIOL × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;10% PEG 2000 monomethyl ether, 0.1M Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.29 Å R-free 0.224 |
| 3LLR Crystal structure of the PWWP domain of Human DNA (cytosine-5-)-methyltransferase 3 alpha Deposited 2010-01-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
275–427(153 aa)
Fragment:PWWP domain (UNP residues 275-427)
|
Not recorded | BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;28% PEG 3,350, 0.1 M ammonium sulfate, 0.1M BisTris, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 2.30 Å R-free 0.256 |
| 3LLR Crystal structure of the PWWP domain of Human DNA (cytosine-5-)-methyltransferase 3 alpha Deposited 2010-01-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain B
275–427(153 aa)
Fragment:PWWP domain (UNP residues 275-427)
|
Not recorded | BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;28% PEG 3,350, 0.1 M ammonium sulfate, 0.1M BisTris, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 2.30 Å R-free 0.256 |
| 3LLR Crystal structure of the PWWP domain of Human DNA (cytosine-5-)-methyltransferase 3 alpha Deposited 2010-01-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain C
275–427(153 aa)
Fragment:PWWP domain (UNP residues 275-427)
|
Not recorded | BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;28% PEG 3,350, 0.1 M ammonium sulfate, 0.1M BisTris, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 2.30 Å R-free 0.256 |
| 3LLR Crystal structure of the PWWP domain of Human DNA (cytosine-5-)-methyltransferase 3 alpha Deposited 2010-01-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain D
275–427(153 aa)
Fragment:PWWP domain (UNP residues 275-427)
|
Not recorded | BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;28% PEG 3,350, 0.1 M ammonium sulfate, 0.1M BisTris, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 2.30 Å R-free 0.256 |
| 3LLR Crystal structure of the PWWP domain of Human DNA (cytosine-5-)-methyltransferase 3 alpha Deposited 2010-01-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain E
275–427(153 aa)
Fragment:PWWP domain (UNP residues 275-427)
|
Not recorded | BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;28% PEG 3,350, 0.1 M ammonium sulfate, 0.1M BisTris, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
|
Resolution 2.30 Å R-free 0.256 |
| 3SVM Human MPP8 - human DNMT3AK47me2 peptide Deposited 2011-07-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric |
Chain P
40–53(14 aa)
Fragment:unp residues 40-53
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;30% polyethylene glycol 1500, 20% polyethylene glycol 400 and 0.1 M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K
|
Resolution 2.31 Å R-free 0.272 |
| 3SVM Human MPP8 - human DNMT3AK47me2 peptide Deposited 2011-07-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain P
40–53(14 aa)
Fragment:unp residues 40-53
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;30% polyethylene glycol 1500, 20% polyethylene glycol 400 and 0.1 M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K
|
Resolution 2.31 Å R-free 0.272 |
| 4QBQ Crystal structure of DNMT3a ADD domain bound to H3 peptide Deposited 2014-05-08 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric |
Chain A
479–610(132 aa)
Fragment:ADD Domain, UNP residues 476-611
Chain C
479–610(132 aa)
Fragment:ADD Domain, UNP residues 476-611
|
Not recorded | ZN ZINC ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.5;291 K;29% PEGMME5000, 0.1M Bis-Tris Propane-HCL, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 2.41 Å R-free 0.230 |
| 4QBR Crystal structure of DNMT3a ADD domain G550D mutant bound to H3 peptide Deposited 2014-05-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric |
Chain A
476–611(136 aa)
Fragment:ADD Domain, UNP residues 476-611
|
Mutation:G550D | ZN ZINC ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;25% PEG3350, 0.1M Bis-Tris-HCL, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 1.90 Å R-free 0.225 |
| 4QBR Crystal structure of DNMT3a ADD domain G550D mutant bound to H3 peptide Deposited 2014-05-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric |
Chain C
476–611(136 aa)
Fragment:ADD Domain, UNP residues 476-611
|
Mutation:G550D | ZN ZINC ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;25% PEG3350, 0.1M Bis-Tris-HCL, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 1.90 Å R-free 0.225 |
| 4QBS Crystal structure of DNMT3a ADD domain E545R mutant bound to H3T3ph peptide Deposited 2014-05-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric |
Chain A
476–611(136 aa)
Fragment:ADD Domain, UNP residues 456-661
|
Mutation:E545R | ZN ZINC ION × 3 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.5;291 K;25% PEG3350, 0.1M Bis-Tris, 0.2M ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 1.80 Å R-free 0.203 |
| 4U7P Crystal structure of DNMT3A-DNMT3L complex Deposited 2014-07-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric |
Chain A
455–912(458 aa)
Fragment:UNP residues 455-912
|
Not recorded | ZN ZINC ION × 3 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION;pH 5.6;291 K;0.05M Bis-Tris, 0.1M Sodium Malonate, 8% PEG3350
|
Resolution 3.82 Å R-free 0.269 |
| 4U7T Crystal structure of DNMT3A-DNMT3L in complex with histone H3 Deposited 2014-07-31 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric |
Chain A
476–912(437 aa)
Fragment:UNP residues 476-912
Chain C
476–912(437 aa)
Fragment:UNP residues 476-912
|
Not recorded | ZN ZINC ION × 6 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;291 K;0.1M Sodium Acetate, 0.6M Ammonium Sulfate
|
Resolution 2.90 Å R-free 0.261 |
| 5YX2 Crystal structure of DNMT3A-DNMT3L in complex with DNA containing two CpG sites Deposited 2017-12-01 | Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 4 PDB declaration: hexameric |
Chain A
628–912(285 aa)
Chain D
628–912(285 aa)
|
Not recorded | GOL GLYCEROL × 6 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;0.1 M Tris-HCl (pH 7.0), 200 mM NaH2PO4, 5% PEG 4000
|
Resolution 2.65 Å R-free 0.222 |
| 6BRR Crystal structure of DNMT3A (R836A)-DNMT3L in complex with DNA containing two CpG sites Deposited 2017-11-30 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 4 PDB declaration: hexameric |
Chain A
439–723(285 aa)
Chain D
439–723(285 aa)
|
Mutation:R836A Mutation:R836A | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;277 K;0.1 M Tris-HCl (pH 7.0), 200 mM NaH2PO4 and 5% PEG4000
|
Resolution 2.97 Å R-free 0.242 |
| 6F57 Crystal structure of DNMT3A-DNMT3L in complex with single CpG-containing DNA Deposited 2017-12-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 2 PDB declaration: tetrameric |
Chain A
628–912(285 aa)
|
Not recorded | SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;296 K;7% PEG4000, 0.1 M Tris-HCl
(pH 8.5), 100 mM MgCl2, 166 mM imidazole (pH 7.0)
|
Resolution 3.10 Å R-free 0.242 |
| 6F57 Crystal structure of DNMT3A-DNMT3L in complex with single CpG-containing DNA Deposited 2017-12-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein–DNA Heteromer;Protein × 2 PDB declaration: tetrameric |
Chain D
628–912(285 aa)
|
Not recorded | SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;296 K;7% PEG4000, 0.1 M Tris-HCl
(pH 8.5), 100 mM MgCl2, 166 mM imidazole (pH 7.0)
|
Resolution 3.10 Å R-free 0.242 |
| 6PA7 The cryo-EM structure of the human DNMT3A2-DNMT3B3 complex bound to nucleosome. Deposited 2019-06-11 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 12 PDB declaration: tetradecameric |
Chain K
224–912(689 aa)
Chain P
224–912(689 aa)
|
Not recorded | CL CHLORIDE ION × 3 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.94 Å |
| 6W8B Structure of DNMT3A in complex with CGA DNA Deposited 2020-03-20 | Different ligand/ion Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 4 PDB declaration: hexameric |
Chain A
628–912(285 aa)
Chain D
628–912(285 aa)
|
Not recorded | 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 2.40 Å R-free 0.233 |
| 6W8B Structure of DNMT3A in complex with CGA DNA Deposited 2020-03-20 | Different ligand/ion Different structure-quality metrics | Assembly 2 Protein–DNA Heteromer;Protein × 4 PDB declaration: hexameric |
Chain H
628–912(285 aa)
Chain K
628–912(285 aa)
|
Not recorded | 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 2.40 Å R-free 0.233 |
| 6W8D Structure of DNMT3A (R882H) in complex with CGT DNA Deposited 2020-03-20 | Different ligand/ion Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 4 PDB declaration: hexameric |
Chain A
628–912(285 aa)
Chain D
628–912(285 aa)
|
Not recorded | 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 2.60 Å R-free 0.253 |
| 6W8J Structure of DNMT3A (R882H) in complex with CAG DNA Deposited 2020-03-20 | Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 4 PDB declaration: hexameric |
Chain A
628–912(285 aa)
Chain D
628–912(285 aa)
|
Not recorded | 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 4.4, 0.2 % PEG8000
|
Resolution 2.44 Å R-free 0.223 |
| 8BA5 Crystal structure of the DNMT3A ADD domain Deposited 2022-10-11 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
476–614(139 aa)
|
Not recorded | EDO 1,2-ETHANEDIOL × 2 ZN ZINC ION × 3 MG MAGNESIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION;291.15 K;17 % PEG 8000, 0.2 M Magnesiumsulfat, 0.1 M TRIS-HCl pH 7.5
|
Resolution 1.45 Å R-free 0.213 |
| 8QZM Structure of DNMT3A1 UDR region bound to H2AK119ub nucleosome Deposited 2023-10-27 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 9 PDB declaration: undecameric |
Chain K
1–912(912 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5;15 mM HEPES pH 7.5, 65 mM NaCl, 1 mM DTT, 0.1 mM S-Adenosyl methionine
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.10 Å |
| 8TDR Crystal structure of the methyltransferase domain of DNMT3A homotetramer Deposited 2023-07-04 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric |
Chain A
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain B
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain E
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain F
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
|
Not recorded | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;277 K;0.2-0.4 M potassium sodium tartrate
|
Resolution 3.32 Å R-free 0.240 |
| 8TDR Crystal structure of the methyltransferase domain of DNMT3A homotetramer Deposited 2023-07-04 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric |
Chain C
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain D
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain G
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain H
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
|
Not recorded | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;277 K;0.2-0.4 M potassium sodium tartrate
|
Resolution 3.32 Å R-free 0.240 |
| 8TE1 Crystal structure of the methyltransferase domain of R882H/R676K DNMT3A homotetramer Deposited 2023-07-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric |
Chain A
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain B
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain E
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain F
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
|
Mutation:R882H,R676K Mutation:R882H,R676K Mutation:R882H,R676K Mutation:R882H,R676K | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 GOL GLYCEROL × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;277 K;0.2-0.4 M potassium sodium tartrate
|
Resolution 2.48 Å R-free 0.226 |
| 8TE1 Crystal structure of the methyltransferase domain of R882H/R676K DNMT3A homotetramer Deposited 2023-07-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric |
Chain C
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain D
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain G
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain H
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
|
Mutation:R882H,R676K Mutation:R882H,R676K Mutation:R882H,R676K Mutation:R882H,R676K | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 GOL GLYCEROL × 5 TLA L(+)-TARTARIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;277 K;0.2-0.4 M potassium sodium tartrate
|
Resolution 2.48 Å R-free 0.226 |
| 8TE3 Crystal structure of the methyltransferase domain of R882C/R676K DNMT3A homotetramer Deposited 2023-07-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric |
Chain A
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain B
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain E
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain F
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
|
Mutation:R882C,R676K Mutation:R882C,R676K Mutation:R882C,R676K Mutation:R882C,R676K | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;277 K;0.2-0.4 M potassium sodium tartrate
|
Resolution 3.20 Å R-free 0.241 |
| 8TE3 Crystal structure of the methyltransferase domain of R882C/R676K DNMT3A homotetramer Deposited 2023-07-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric |
Chain C
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain D
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain G
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain H
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
|
Mutation:R882C,R676K Mutation:R882C,R676K Mutation:R882C,R676K Mutation:R882C,R676K | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;277 K;0.2-0.4 M potassium sodium tartrate
|
Resolution 3.20 Å R-free 0.241 |
| 8TE4 Crystal structure of the methyltransferase domain of R882H/N879A DNMT3A homotetramer Deposited 2023-07-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric |
Chain A
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain B
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain E
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain F
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
|
Mutation:R882H,N879A Mutation:R882H,N879A Mutation:R882H,N879A Mutation:R882H,N879A | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 GOL GLYCEROL × 10 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;277 K;0.2-0.4 M potassium sodium tartrate
|
Resolution 2.65 Å R-free 0.236 |
| 8TE4 Crystal structure of the methyltransferase domain of R882H/N879A DNMT3A homotetramer Deposited 2023-07-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric |
Chain C
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain D
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain G
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
Chain H
628–912(285 aa)
Fragment:methyltransferase domain (UNP residues 628-912)
|
Mutation:R882H,N879A Mutation:R882H,N879A Mutation:R882H,N879A Mutation:R882H,N879A | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 GOL GLYCEROL × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;277 K;0.2-0.4 M potassium sodium tartrate
|
Resolution 2.65 Å R-free 0.236 |
| 8U5H Cryo-EM structure of human DNMT3A UDR bound to H2AK119ub1-modified nucleosome Deposited 2023-09-12 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 11 PDB declaration: tridecameric |
Chain A
126–223(98 aa)
Chain B
126–223(98 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.23 Å |
| 8UW1 Cryo-EM structure of DNMT3A1 UDR in complex with H2AK119Ub-nucleosome Deposited 2023-11-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 9 PDB declaration: undecameric |
Chain K
159–228(70 aa)
|
Not recorded | No recorded non-water small molecule |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.9;50 mM HEPES pH 7.9, 100 mM NaCl, 2 mM DTT
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.88 Å |
| 9E00 Cryo-EM structure of human DNMT3A2-DNMT3B3 complex bound to di-nucleosome Deposited 2024-10-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 24 PDB declaration: 26-meric |
Chain K
224–912(689 aa)
Chain U
224–912(689 aa)
Chain W
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.75 Å |
| 9E05 The consensus model of the cryo-EM structure of human DNMT3A2-DNMT3B3 complex bound to di-nucleosome Deposited 2024-10-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 24 PDB declaration: 26-meric |
Chain K
224–912(689 aa)
Chain U
224–912(689 aa)
Chain W
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 18 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 8.00 Å |
| 9E0F A focus of DNMT tetramer (1) of the cryo-EM structure of human DNMT3A2-DNMT3B3 complex bound to di-nucleosome Deposited 2024-10-17 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain U
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.46 Å |
| 9E0G A focus of tetramer (2) of the cryo-EM structure of human DNMT3A2-DNMT3B3 complex bound to di-nucleosome Deposited 2024-10-17 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain K
224–912(689 aa)
Chain W
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.72 Å |
| 9E2D Cryo-EM structure of human DNMT3A2-DNMT3B3 complex bound to a di-nucleosome with a five base pair linker Deposited 2024-10-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 24 PDB declaration: 26-meric |
Chain K
224–912(689 aa)
Chain U
224–912(689 aa)
Chain W
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 18 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 6.08 Å |
| 9E2Q Cryo-EM structure of DNMT 3A2/3B3 tetramer in complex with a di-nucleosome with a six base pair linker Deposited 2024-10-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 24 PDB declaration: 26-meric |
Chain K
224–912(689 aa)
Chain U
224–912(689 aa)
Chain W
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 18 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.14 Å |
| 9E2R Cryo-EM structure of human DNMT3A2-DNMT3B3 complex bound to a di-nucleosome and an histone-3 peptide Deposited 2024-10-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 24 PDB declaration: 26-meric |
Chain K
224–912(689 aa)
Chain U
224–912(689 aa)
Chain W
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 18 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 7.71 Å |
| 9E3D Cryo-EM structure of DNMT 3A2/3B3 tetramer in complex with a di-nucleosome with K120R mutant H2B Deposited 2024-10-23 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 20 PDB declaration: 22-meric |
Chain U
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.80 Å |
| 9E3R Cryo-EM structure of PWWP domain deleted DNMT 3A2/3B3 in complex with a di-nucleosome Deposited 2024-10-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 24 PDB declaration: 26-meric |
Chain K
224–912(689 aa)
Chain U
224–912(689 aa)
Chain W
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 18 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 6.90 Å |
| 9E3U Cryo-EM structure of DNMT 3A2/3B3 tetramer bound to a di-nucleosome with a 25 base-pair linker Deposited 2024-10-24 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 13 PDB declaration: 15-meric |
Chain U
224–912(689 aa)
Chain Y
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 9 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 4.90 Å |
| 9LQ1 Structure of human DNMT3A-TCL1A complex Deposited 2025-01-27 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric |
Chain A
1–912(912 aa)
Chain F
1–912(912 aa)
|
Not recorded | ZN ZINC ION × 6 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8;25mM Tris pH 8.0, 150mM NaCl,5 mM DTT
cryo-EM vitrification conditions
Cryogen ETHANE;Vitrification carried out in argon atmosphere
|
Resolution 3.36 Å |
| 9MP0 The cryo-EM structure of the human DNA methyltransferases DNMT3A2 and DNMT3L dodecamer Deposited 2024-12-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 10 PDB declaration: decameric |
Chain L
224–912(689 aa)
Chain M
224–912(689 aa)
Chain N
224–912(689 aa)
Chain O
224–912(689 aa)
Chain R
224–912(689 aa)
Chain S
224–912(689 aa)
Chain T
224–912(689 aa)
Chain U
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 30 SAH S-ADENOSYL-L-HOMOCYSTEINE × 8 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.66 Å |
| 9MPO The cryo-EM structure of the human DNA methyltransferase DNMT3A2 and DNMT3L octamer Deposited 2024-12-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer;Protein × 6 PDB declaration: hexameric |
Chain A
224–912(689 aa)
Chain B
224–912(689 aa)
Chain C
224–912(689 aa)
Chain D
224–912(689 aa)
Chain E
224–912(689 aa)
Chain F
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 12 SAH S-ADENOSYL-L-HOMOCYSTEINE × 6 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.62 Å |
| 9MPP The cryo-EM structure of nucleosome-bound DNA methyltransferases DNMT3A2 and DNMT3L Deposited 2024-12-31 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 12 PDB declaration: 14-meric |
Chain K
224–912(689 aa)
Chain M
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 6 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.10 Å |
| 9PRW Cryo-EM structure of human DNMT3A/3L Deposited 2025-07-24 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain A
281–912(632 aa)
Chain D
281–912(632 aa)
|
Not recorded | SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 ZN ZINC ION × 12 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.66 Å |
| 9Q7U Composite map for Cryo-EM structure of DNMT3A2-DNMT3B3 tetramer bound to 167H3K36me2-nucleosome Deposited 2025-08-25 | Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 12 PDB declaration: 14-meric |
Chain K
224–912(689 aa)
Chain L
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 9 SAO 5'-S-[(3S)-3-azaniumyl-3-carboxypropyl]-5'-thioadenosine × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.40 Å |
| 9Y4P Cryo-EM structure of DNMT3A2/3B3 in complex with H3K36me2 di-nucleosome with eight base pair linker Deposited 2025-09-03 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein–DNA Heteromer;Protein × 24 PDB declaration: 26-meric |
Chain a
224–912(689 aa)
Chain c
224–912(689 aa)
Chain d
224–912(689 aa)
Chain f
224–912(689 aa)
|
Not recorded | ZN ZINC ION × 18 SAH S-ADENOSYL-L-HOMOCYSTEINE × 4 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.8
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.84 Å |
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 |