2pb7

Crystal Structure of the SRA domain of the human UHRF1 protein

Method: X-RAY DIFFRACTION Dmax: 60.6 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 408–643 Fragment:SRA domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;14-19% PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.90 Å R-free 0.227

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 4–239; UniProt 408–643

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 2pb7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2pb7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2pb7
Deposition date deposition_date2007-03-28
Structure title titleCrystal Structure of the SRA domain of the human UHRF1 protein
Keywords keywordsbeta barrel, new fold, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.65
Radius of gyration Rg (electron density) rg_electron16.61
Forward intensity I(0) i08884730.00
Molecular weight molecular_weight21035.0 kDa
Excluded volume excluded_volume25904 ų
Envelope volume envelope_volume30279 ų
Hydration-shell volume shell_volume15478 ų
Envelope diameter envelope_diameter61.0
Shell Rg shell_rg22.62
Envelope Rg envelope_rg17.13
Shape Rg shape_rg16.59
Total Rg total_rg17.66
Total atoms total_atoms1488
Residues n_residues197
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 dmax60.6
Rg (real space) rg_real17.60
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real8.8850e+06
I(0) uncertainty (real space) i0_real_error1.0650e+05
Rg (reciprocal space) rg_reciprocal17.61
I(0) (reciprocal space) i0_reciprocal8885000.0000
Solution quality estimate total_estimate0.7864
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.131
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2005000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.746; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2pb7a1
Class classb — All beta proteins
Fold Fold foldb.122 — PUA domain-like
Superfamily Superfamily superfamilyb.122.1 — PUA domain-like
Family Family familyb.122.1.12 — SRA domain-like

CATH v4.4 (1 domains)

Domain ID domain_id2pb7A01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology280 — PUA domain-like
Homologous superfamily homologous superfamily10 — SRA-YDG

8. Citations (1)

9. Files and Curves (10)