7lmk

Crystal structure of bovine DNMT1 BAH1 domain in complex with H4K20me3

Method: X-RAY DIFFRACTION Dmax: 158.1 Å Quality: GOOD

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

DNA (cytosine-5)-methyltransferase 1

Bos taurus

UniProt Q24K09

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 725–837 Chain A; UniProt 859–897 Not recorded Histone H4 × 1 (P62805) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;13% PEG1500, 20 mM DTT and 200 mM L-proline, 0.1 M HEPES (pH 7.5) Resolution 2.65 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 725–837 Chain B; UniProt 859–897 Not recorded Histone H4 × 1 (P62805) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;13% PEG1500, 20 mM DTT and 200 mM L-proline, 0.1 M HEPES (pH 7.5) Resolution 2.65 Å R-free 0.258
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 725–837 Chain C; UniProt 859–897 Not recorded Histone H4 × 1 (P62805) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;13% PEG1500, 20 mM DTT and 200 mM L-proline, 0.1 M HEPES (pH 7.5) Resolution 2.65 Å R-free 0.258
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 725–837 Chain D; UniProt 859–897 Not recorded Histone H4 × 1 (P62805) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;13% PEG1500, 20 mM DTT and 200 mM L-proline, 0.1 M HEPES (pH 7.5) Resolution 2.65 Å R-free 0.258

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.

2 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNMT1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–114; UniProt 725–837 Author chain A; PDBConstruct 120–158; UniProt 859–897 Author chain B; PDBConstruct 2–114; UniProt 725–837 Author chain B; PDBConstruct 120–158; UniProt 859–897 Author chain C; PDBConstruct 2–114; UniProt 725–837 Author chain C; PDBConstruct 120–158; UniProt 859–897 Author chain D; PDBConstruct 2–114; UniProt 725–837 Author chain D; PDBConstruct 120–158; UniProt 859–897

Histone H4

OrganismNot specified

UniProt P62805

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 F; UniProt 15–27 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA (cytosine-5)-methyltransferase 1 × 1 (Q24K09) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;13% PEG1500, 20 mM DTT and 200 mM L-proline, 0.1 M HEPES (pH 7.5) Resolution 2.65 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 15–27 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA (cytosine-5)-methyltransferase 1 × 1 (Q24K09) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;13% PEG1500, 20 mM DTT and 200 mM L-proline, 0.1 M HEPES (pH 7.5) Resolution 2.65 Å R-free 0.258
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 15–27 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA (cytosine-5)-methyltransferase 1 × 1 (Q24K09) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;13% PEG1500, 20 mM DTT and 200 mM L-proline, 0.1 M HEPES (pH 7.5) Resolution 2.65 Å R-free 0.258
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 15–27 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA (cytosine-5)-methyltransferase 1 × 1 (Q24K09) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;13% PEG1500, 20 mM DTT and 200 mM L-proline, 0.1 M HEPES (pH 7.5) Resolution 2.65 Å R-free 0.258

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.

581 other PDB entries and 630 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–13; UniProt 15–27 Author chain G; PDBConstruct 1–13; UniProt 15–27 Author chain H; PDBConstruct 1–13; UniProt 15–27 Author chain I; PDBConstruct 1–13; UniProt 15–27

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 7lmk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7lmk
Deposition date deposition_date2021-02-05
Structure title titleCrystal structure of bovine DNMT1 BAH1 domain in complex with H4K20me3
Keywords keywordsDNA methylation, DNA methyltransferase 1, Histone modification, Allosteric regulation, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.55
Radius of gyration Rg (electron density) rg_electron42.75
Forward intensity I(0) i086699900.00
Molecular weight molecular_weight72800.0 kDa
Excluded volume excluded_volume90362 ų
Envelope volume envelope_volume179510 ų
Hydration-shell volume shell_volume38117 ų
Envelope diameter envelope_diameter165.0
Shell Rg shell_rg42.76
Envelope Rg envelope_rg43.35
Shape Rg shape_rg42.84
Total Rg total_rg42.44
Total atoms total_atoms5117
Residues n_residues653
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 dmax158.1
Rg (real space) rg_real43.00
Rg uncertainty (real space) rg_real_error2.18
I(0) (real space) i0_real8.6700e+07
I(0) uncertainty (real space) i0_real_error1.7690e+06
Rg (reciprocal space) rg_reciprocal42.56
I(0) (reciprocal space) i0_reciprocal86660000.0000
Solution quality estimate total_estimate0.7549
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary51.3
Skewness Skewness skewness0.697
Kurtosis Kurtosis kurtosis0.582
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4690000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.455; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.502

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)