4z96

Crystal structure of DNMT1 in complex with USP7

Method: X-RAY DIFFRACTION Dmax: 126.5 Å Quality: REASONABLE

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 544–1067 Fragment:UNP residues 544-1067 DNA (cytosine-5)-methyltransferase 1 × 1 (P26358) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;0.1 M sodium citrate, pH5.5, 10% PEG6000, 15% glycerol Resolution 2.85 Å R-free 0.246

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 Q93009-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–530; UniProt 544–1067

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 C; UniProt 1097–1129 Fragment:UNP residues 1097-1129 Ubiquitin carboxyl-terminal hydrolase 7 × 1 (Q93009) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;0.1 M sodium citrate, pH5.5, 10% PEG6000, 15% glycerol Resolution 2.85 Å R-free 0.246

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 C; PDBConstruct 1–33; UniProt 1097–1129

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 4z96

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4z96
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4z96
Deposition date deposition_date2015-04-09
Structure title titleCrystal structure of DNMT1 in complex with USP7
Keywords keywordsUSP7, DNMT1, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.73
Radius of gyration Rg (electron density) rg_electron41.39
Forward intensity I(0) i053204900.00
Molecular weight molecular_weight57951.0 kDa
Excluded volume excluded_volume72231 ų
Envelope volume envelope_volume110990 ų
Hydration-shell volume shell_volume26023 ų
Envelope diameter envelope_diameter134.1
Shell Rg shell_rg39.35
Envelope Rg envelope_rg40.80
Shape Rg shape_rg41.43
Total Rg total_rg41.12
Total atoms total_atoms4084
Residues n_residues529
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 dmax126.5
Rg (real space) rg_real41.29
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real5.3200e+07
I(0) uncertainty (real space) i0_real_error9.3660e+05
Rg (reciprocal space) rg_reciprocal40.74
I(0) (reciprocal space) i0_reciprocal53170000.0000
Solution quality estimate total_estimate0.6549
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.482
Kurtosis Kurtosis kurtosis-0.875
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3848000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.451; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.158; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4z96A01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id4z96A02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)