5lnb

Crystal structure of the de-sumoylating protease

Method: X-RAY DIFFRACTION Dmax: 67.3 Å Quality: GOOD

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

Ubiquitin-like-specific protease 2

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P40537

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 B; UniProt 411–710 Not recorded ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M di-ammonium hydrogen citrate, 20 % PEG 3350, protein concentration 3 mg/ml Resolution 2.30 Å R-free 0.197

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 ULP2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 2–301; UniProt 411–710

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 5lnb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5lnb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5lnb
Deposition date deposition_date2016-08-03
Structure title titleCrystal structure of the de-sumoylating protease
Keywords keywordsProtease, de-sumoylation, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.57
Radius of gyration Rg (electron density) rg_electron19.48
Forward intensity I(0) i015294700.00
Molecular weight molecular_weight30876.0 kDa
Excluded volume excluded_volume39327 ų
Envelope volume envelope_volume46097 ų
Hydration-shell volume shell_volume19946 ų
Envelope diameter envelope_diameter69.5
Shell Rg shell_rg25.77
Envelope Rg envelope_rg19.98
Shape Rg shape_rg19.43
Total Rg total_rg20.60
Total atoms total_atoms2181
Residues n_residues259
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 dmax67.3
Rg (real space) rg_real20.52
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.5290e+07
I(0) uncertainty (real space) i0_real_error1.9090e+05
Rg (reciprocal space) rg_reciprocal20.53
I(0) (reciprocal space) i0_reciprocal15290000.0000
Solution quality estimate total_estimate0.8080
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.224
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3273000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)