9k2x

Cryo-EM structure of USP7:DNMT1 complex; open conformation

Method: ELECTRON MICROSCOPY Dmax: 146.9 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 7

Homo sapiens

UniProt Q93009

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 1–1102 Not recorded DNA (cytosine-5)-methyltransferase 1 × 1 (P26358) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 Å

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.

84 other PDB entries and 145 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–1107; UniProt 1–1102

DNA (cytosine-5)-methyltransferase 1

Homo sapiens

UniProt P26358

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 B; UniProt 351–1616 Not recorded Ubiquitin carboxyl-terminal hydrolase 7 × 1 (Q93009) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 Å

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.

24 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNMT1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–1271; UniProt 351–1616

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 9k2x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9k2x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9k2x
Deposition date deposition_date2024-10-18
Structure title titleCryo-EM structure of USP7:DNMT1 complex; open conformation
Keywords keywordsDNA methylation, deubiquitination, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.34
Radius of gyration Rg (electron density) rg_electron43.12
Forward intensity I(0) i0468334000.00
Molecular weight molecular_weight175960.0 kDa
Excluded volume excluded_volume219620 ų
Envelope volume envelope_volume321090 ų
Hydration-shell volume shell_volume63401 ų
Envelope diameter envelope_diameter152.2
Shell Rg shell_rg46.74
Envelope Rg envelope_rg43.05
Shape Rg shape_rg43.11
Total Rg total_rg43.35
Total atoms total_atoms12376
Residues n_residues1551
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 dmax146.9
Rg (real space) rg_real43.38
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real4.6830e+08
I(0) uncertainty (real space) i0_real_error9.7430e+06
Rg (reciprocal space) rg_reciprocal43.34
I(0) (reciprocal space) i0_reciprocal468300000.0000
Solution quality estimate total_estimate0.8838
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.0
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49050000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.864

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)