2lgg

Structure of PHD domain of UHRF1 in complex with H3 peptide

Method: SOLUTION NMR Dmax: 46.6 Å Quality: GOOD

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 298–366 Fragment:UNP RESIDUES 298-366 histone H3 peptide × 1 ZN ZINC ION × 3 SOLUTION NMR NMR measurement conditions:pH 7.4;293 K;Ionic strength (raw mmCIF value) 0.15;Pressure ambient NMR sample composition:1 mM [U-100% 13C; U-100% 15N] entity_1-1, 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 1–69; UniProt 298–366

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 2lgg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lgg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lgg
Deposition date deposition_date2011-07-26
Structure title titleStructure of PHD domain of UHRF1 in complex with H3 peptide
Keywords keywordsDNA Binding Protein/gene Regulation, LIGASE-DNA BINDING PROTEIN complex; LIGASE/DNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.86
Radius of gyration Rg (electron density) rg_electron12.83
Forward intensity I(0) i0670223000.00
Molecular weight molecular_weight186770.0 kDa
Excluded volume excluded_volume220060 ų
Envelope volume envelope_volume24681 ų
Hydration-shell volume shell_volume13872 ų
Envelope diameter envelope_diameter51.1
Shell Rg shell_rg20.92
Envelope Rg envelope_rg15.32
Shape Rg shape_rg12.90
Total Rg total_rg12.78
Total atoms total_atoms24300
Residues n_residues1620
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 dmax46.6
Rg (real space) rg_real12.84
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real6.7020e+08
I(0) uncertainty (real space) i0_real_error8.3630e+06
Rg (reciprocal space) rg_reciprocal12.85
I(0) (reciprocal space) i0_reciprocal670200000.0000
Solution quality estimate total_estimate0.7699
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.9
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.155
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha136800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lggA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)

8. Citations (1)

9. Files and Curves (10)