1yy6

The Crystal Structure of the N-terminal domain of HAUSP/USP7 complexed with an EBNA1 peptide

Method: X-RAY DIFFRACTION Dmax: 56.0 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 7

Homo sapiens

UniProt Q93009

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 54–204 Not recorded Epstein-Barr nuclear antigen-1 × 1 NA SODIUM ION × 21 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;298 K;30 % PEG 4000, 0.1 M Tris pH 8.5, 0.2 M lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.70 Å R-free 0.230

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.

84 other PDB entries and 145 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–154; UniProt 54–204

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 1yy6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1yy6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1yy6
Deposition date deposition_date2005-02-23
Structure title titleThe Crystal Structure of the N-terminal domain of HAUSP/USP7 complexed with an EBNA1 peptide
Keywords keywordsTRAF-domain, peptide binding site, protein peptide complex, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.84
Radius of gyration Rg (electron density) rg_electron15.59
Forward intensity I(0) i04953580.00
Molecular weight molecular_weight17248.0 kDa
Excluded volume excluded_volume21875 ų
Envelope volume envelope_volume23872 ų
Hydration-shell volume shell_volume13261 ų
Envelope diameter envelope_diameter57.9
Shell Rg shell_rg21.07
Envelope Rg envelope_rg16.05
Shape Rg shape_rg15.58
Total Rg total_rg16.65
Total atoms total_atoms1207
Residues n_residues145
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 dmax56.0
Rg (real space) rg_real16.83
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real4.9540e+06
I(0) uncertainty (real space) i0_real_error6.0270e+04
Rg (reciprocal space) rg_reciprocal16.83
I(0) (reciprocal space) i0_reciprocal4954000.0000
Solution quality estimate total_estimate0.7988
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary19.6
Skewness Skewness skewness0.330
Kurtosis Kurtosis kurtosis-0.276
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1121000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id1yy6A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology210 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Homologous superfamily homologous superfamily10 — Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A

8. Citations (1)

9. Files and Curves (10)