6ved

Solution structure of the TTD and linker region of UHRF1

Method: SOLUTION NMR Dmax: 48.8 Å Quality: REASONABLE

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 146–313 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.5;303 K;Ionic strength (raw mmCIF value) 150;Pressure 1 NMR sample composition:250 uM [U-99% 13C; U-99% 15N] TTD-linker, 150 mM sodium chloride, 25 mM sodium phosphate, 5 mM DTT, 2 mM beta-mercaptoethanol, 2 mM TCEP, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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 Q96T88-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–168; UniProt 146–313

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 6ved

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ved
Deposition date deposition_date2019-12-31
Structure title titleSolution structure of the TTD and linker region of UHRF1
Keywords keywordsHistone, Tandem Tudor Domain, UHRF1, H3K9me3, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.11
Radius of gyration Rg (electron density) rg_electron17.94
Forward intensity I(0) i02298870000.00
Molecular weight molecular_weight388260.0 kDa
Excluded volume excluded_volume478240 ų
Envelope volume envelope_volume56719 ų
Hydration-shell volume shell_volume22440 ų
Envelope diameter envelope_diameter83.4
Shell Rg shell_rg28.59
Envelope Rg envelope_rg22.40
Shape Rg shape_rg17.89
Total Rg total_rg18.28
Total atoms total_atoms53780
Residues n_residues3360
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 dmax48.8
Rg (real space) rg_real17.00
Rg uncertainty (real space) rg_real_error0.08
I(0) (real space) i0_real2.1880e+09
I(0) uncertainty (real space) i0_real_error2.1340e+07
Rg (reciprocal space) rg_reciprocal18.27
I(0) (reciprocal space) i0_reciprocal2299000000.0000
Solution quality estimate total_estimate0.6830
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.1
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha2.7360
Highest regularization parameter α highest_alpha1832000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.004; Oscil: 0.970; Stabil: 0.990; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6vedA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily140
Domain ID domain_id6vedA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily30

8. Citations (1)

9. Files and Curves (10)