8q00

TssM-Ub-PA complex - A USP-like DUB from B. pseudomallei (193-430) reacted with Ub-PA

Method: X-RAY DIFFRACTION Dmax: 104.3 Å Quality: REASONABLE

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

TssM

Burkholderia pseudomallei

UniProt D7SFB8

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 192–490 Not recorded Polyubiquitin-B × 1 (P0CG47) FLC CITRATE ANION × 1 EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.2 M ammonium citrate dibasic and 22 % w/v PEG 3350; 1:2, 1:1, 2:1 protein:reservoir ration; cryoprotected with reservoir + 25% ethylene glycol Resolution 1.62 Å R-free 0.198
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 192–490 Not recorded Polyubiquitin-B × 1 (P0CG47) EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.2 M ammonium citrate dibasic and 22 % w/v PEG 3350; 1:2, 1:1, 2:1 protein:reservoir ration; cryoprotected with reservoir + 25% ethylene glycol Resolution 1.62 Å R-free 0.198

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 D7SFB8_BURPE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–300; UniProt 192–490 Author chain C; PDBConstruct 2–300; UniProt 192–490

Polyubiquitin-B

Homo sapiens

UniProt P0CG47

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 1–76 Non-standard monomer:Yes (specific site not provided by mmCIF) TssM × 1 (D7SFB8) FLC CITRATE ANION × 1 EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.2 M ammonium citrate dibasic and 22 % w/v PEG 3350; 1:2, 1:1, 2:1 protein:reservoir ration; cryoprotected with reservoir + 25% ethylene glycol Resolution 1.62 Å R-free 0.198
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–76 Non-standard monomer:Yes (specific site not provided by mmCIF) TssM × 1 (D7SFB8) EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.2 M ammonium citrate dibasic and 22 % w/v PEG 3350; 1:2, 1:1, 2:1 protein:reservoir ration; cryoprotected with reservoir + 25% ethylene glycol Resolution 1.62 Å R-free 0.198

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.

278 other PDB entries and 428 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain D; PDBConstruct 1–76; UniProt 1–76

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 8q00

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8q00
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8q00
Deposition date deposition_date2023-07-27
Structure title titleTssM-Ub-PA complex - A USP-like DUB from B. pseudomallei (193-430) reacted with Ub-PA
Keywords keywordsDeubiquitinase, papain-fold, USP, HYDROLASE, Ub-PA; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.08
Radius of gyration Rg (electron density) rg_electron31.46
Forward intensity I(0) i0106150000.00
Molecular weight molecular_weight81212.0 kDa
Excluded volume excluded_volume101590 ų
Envelope volume envelope_volume127770 ų
Hydration-shell volume shell_volume35004 ų
Envelope diameter envelope_diameter110.3
Shell Rg shell_rg36.88
Envelope Rg envelope_rg31.21
Shape Rg shape_rg31.42
Total Rg total_rg32.05
Total atoms total_atoms5727
Residues n_residues745
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 dmax104.3
Rg (real space) rg_real32.06
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.0610e+08
I(0) uncertainty (real space) i0_real_error1.6150e+06
Rg (reciprocal space) rg_reciprocal32.07
I(0) (reciprocal space) i0_reciprocal106200000.0000
Solution quality estimate total_estimate0.6873
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.3
Skewness Skewness skewness0.280
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15690000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 0.096; Positv: 1.000; Valcen: 0.992; Smooth: 0.861

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)