9yc2

Crystal structure of USP49 ZnF-UBP domain

Method: X-RAY DIFFRACTION Dmax: 45.2 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 49

Homo sapiens

UniProt Q70CQ1

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 1–103 Not recorded SO4 SULFATE ION × 2 GOL GLYCEROL × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;281 K;0.2 M sodium chloride; 2 M ammonium sulphate; 0.1 M sodium cacodylate Resolution 1.40 Å R-free 0.192

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name UBP49_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–105; UniProt 1–103

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 9yc2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yc2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yc2
Deposition date deposition_date2025-09-18
最后修订 last_revision2025-10-29
Structure title titleCrystal structure of USP49 ZnF-UBP domain
Keywords keywordsUSP49, deubiquitinase, DUB, protease, ubiquitin, histone, nucleosome, ubiquitin binding domain, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.47
Radius of gyration Rg (electron density) rg_electron13.13
Forward intensity I(0) i03660050.00
Molecular weight molecular_weight12470.0 kDa
Excluded volume excluded_volume15178 ų
Envelope volume envelope_volume17377 ų
Hydration-shell volume shell_volume11288 ų
Envelope diameter envelope_diameter44.0
Shell Rg shell_rg18.87
Envelope Rg envelope_rg13.42
Shape Rg shape_rg13.10
Total Rg total_rg14.42
Total atoms total_atoms1677
Residues n_residues105
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 dmax45.2
Rg (real space) rg_real14.38
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real3.6600e+06
I(0) uncertainty (real space) i0_real_error3.7570e+04
Rg (reciprocal space) rg_reciprocal14.39
I(0) (reciprocal space) i0_reciprocal3660000.0000
Solution quality estimate total_estimate0.8994
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.7
Skewness Skewness skewness0.117
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha501400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)