2l3r

NMR structure of UHRF1 Tandem Tudor Domains in a complex with Histone H3 peptide

Method: SOLUTION NMR Dmax: 49.5 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 126–285 Fragment:unp residues 126-285 Histone H3 × 1 (Q3BDD9) SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 250;Pressure 1 NMR sample composition:0.6 mM [U-100% 15N] protein, 0.6 mM [U-100% 13C] protein, 3 mM protein, 90% H2O/10% D2O | 90% H2O/10% 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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–162; UniProt 126–285

Histone H3

OrganismNot specified

UniProt Q3BDD9

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 2–12 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase UHRF1 × 1 (Q96T88) SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 250;Pressure 1 NMR sample composition:0.6 mM [U-100% 15N] protein, 0.6 mM [U-100% 13C] protein, 3 mM protein, 90% H2O/10% D2O | 90% H2O/10% 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q3BDD9_9INSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–11; UniProt 2–12

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 2l3r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2l3r
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2l3r
Deposition date deposition_date2010-09-21
Structure title titleNMR structure of UHRF1 Tandem Tudor Domains in a complex with Histone H3 peptide
Keywords keywords;tudor domain, heterochromatin, transcriptional repression, Structural Genomics, Structural Genomics Consortium, SGC, DNA BINDING PROTEIN, DNA BINDING PROTEIN-GENE REGULATION complex ;; DNA BINDING PROTEIN/GENE REGULATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.15
Radius of gyration Rg (electron density) rg_electron17.90
Forward intensity I(0) i01380260000.00
Molecular weight molecular_weight301300.0 kDa
Excluded volume excluded_volume371510 ų
Envelope volume envelope_volume44609 ų
Hydration-shell volume shell_volume19245 ų
Envelope diameter envelope_diameter82.8
Shell Rg shell_rg26.52
Envelope Rg envelope_rg21.28
Shape Rg shape_rg17.83
Total Rg total_rg18.27
Total atoms total_atoms41775
Residues n_residues2565
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 dmax49.5
Rg (real space) rg_real17.00
Rg uncertainty (real space) rg_real_error0.08
I(0) (real space) i0_real1.3140e+09
I(0) uncertainty (real space) i0_real_error1.2340e+07
Rg (reciprocal space) rg_reciprocal18.34
I(0) (reciprocal space) i0_reciprocal1380000000.0000
Solution quality estimate total_estimate0.6801
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.380
Kurtosis Kurtosis kurtosis-0.260
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha2.6770
Highest regularization parameter α highest_alpha1698000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.957; Stabil: 0.990; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; 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_id2l3rA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily140
Domain ID domain_id2l3rA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily30

8. Citations (1)

9. Files and Curves (10)