8bs3

Structure of USP36 in complex with Fubi-PA

Method: X-RAY DIFFRACTION Dmax: 71.3 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 36

Homo sapiens

UniProt Q9P275

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 80–461 Not recorded 40S ribosomal protein S30 × 1 (P62861) ZN ZINC ION × 2 AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291 K;0.1 M MMT buffer pH 7.0, 25% (w/v) PEG 1500 Resolution 2.20 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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP36_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–383; UniProt 80–461

40S ribosomal protein S30

Homo sapiens

UniProt P62861

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 B; UniProt 1–73 Not recorded Ubiquitin carboxyl-terminal hydrolase 36 × 1 (Q9P275) ZN ZINC ION × 2 AYE prop-2-en-1-amine × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291 K;0.1 M MMT buffer pH 7.0, 25% (w/v) PEG 1500 Resolution 2.20 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.

181 other PDB entries and 181 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS30_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–73; UniProt 1–73

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 8bs3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bs3
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8bs3
Deposition date deposition_date2022-11-24
Structure title titleStructure of USP36 in complex with Fubi-PA
Keywords keywordsUSP, USP36, Ubiquitin, Fubi, S30, Fau, probe, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.99
Radius of gyration Rg (electron density) rg_electron20.68
Forward intensity I(0) i032641100.00
Molecular weight molecular_weight43857.0 kDa
Excluded volume excluded_volume54843 ų
Envelope volume envelope_volume63714 ų
Hydration-shell volume shell_volume25171 ų
Envelope diameter envelope_diameter72.3
Shell Rg shell_rg27.93
Envelope Rg envelope_rg20.85
Shape Rg shape_rg20.61
Total Rg total_rg21.79
Total atoms total_atoms3073
Residues n_residues397
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 dmax71.3
Rg (real space) rg_real21.85
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real3.2640e+07
I(0) uncertainty (real space) i0_real_error3.9440e+05
Rg (reciprocal space) rg_reciprocal21.87
I(0) (reciprocal space) i0_reciprocal32640000.0000
Solution quality estimate total_estimate0.8832
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.203
Kurtosis Kurtosis kurtosis-0.279
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha7529000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8bs3A01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily10 — Cysteine proteinases
Domain ID domain_id8bs3B01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)