6b9m

Crystal structure of UHRF1 TTD domain in complex with the polybasic region

Method: X-RAY DIFFRACTION Dmax: 113.5 Å Quality: GOOD

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

E3 ubiquitin-protein ligase UHRF1

Danio rerio

UniProt E7EZF3

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 129–280 Chain B; UniProt 129–280 Chain C; UniProt 129–280 Fragment:unp residues 129-280 E3 ubiquitin-protein ligase UHRF1 × 1 (Q96T88) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1M Succinic acid pH7.0, 15% (v/v) Polyethylene glycol 3350 Resolution 1.68 Å R-free 0.207

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name UHRF1_DANRE
Isoform E7EZF3-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–153; UniProt 129–280 Author chain B; PDBConstruct 2–153; UniProt 129–280 Author chain C; PDBConstruct 2–153; UniProt 129–280

E3 ubiquitin-protein ligase UHRF1

Homo sapiens

UniProt Q96T88

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 638–678 Fragment:unp residues 638-678 E3 ubiquitin-protein ligase UHRF1 × 3 (E7EZF3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;0.1M Succinic acid pH7.0, 15% (v/v) Polyethylene glycol 3350 Resolution 1.68 Å R-free 0.207

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.

44 other PDB entries and 76 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UHRF1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–41; UniProt 638–678

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 6b9m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6b9m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6b9m
Deposition date deposition_date2017-10-10
Structure title titleCrystal structure of UHRF1 TTD domain in complex with the polybasic region
Keywords keywordscomplex, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.33
Radius of gyration Rg (electron density) rg_electron32.71
Forward intensity I(0) i046412600.00
Molecular weight molecular_weight53364.0 kDa
Excluded volume excluded_volume66737 ų
Envelope volume envelope_volume93245 ų
Hydration-shell volume shell_volume26575 ų
Envelope diameter envelope_diameter118.6
Shell Rg shell_rg35.26
Envelope Rg envelope_rg32.70
Shape Rg shape_rg32.69
Total Rg total_rg32.99
Total atoms total_atoms3769
Residues n_residues465
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 dmax113.5
Rg (real space) rg_real32.83
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real4.6410e+07
I(0) uncertainty (real space) i0_real_error6.7070e+05
Rg (reciprocal space) rg_reciprocal32.62
I(0) (reciprocal space) i0_reciprocal46400000.0000
Solution quality estimate total_estimate0.7983
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.590
Kurtosis Kurtosis kurtosis-0.276
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5942000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.707; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.556; Smooth: 0.697

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6b9mA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily30
Domain ID domain_id6b9mB02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily30
Domain ID domain_id6b9mC02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily30

8. Citations (1)

9. Files and Curves (10)