6och

Crystal structure of VASH1-SVBP complex bound with parthenolide

Method: X-RAY DIFFRACTION Dmax: 97.1 Å Quality: GOOD

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

Tubulinyl-Tyr carboxypeptidase 1

Homo sapiens

UniProt Q7L8A9

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 61–302 Not recorded Small vasohibin-binding protein × 1 (Q8N300) M4Y parthenolide × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;0.2 M ammonium sulfate, 0.1 M Bis-tris, pH 5.5, and 25 % (w/v) PEG 3350 Resolution 2.00 Å R-free 0.229
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 61–302 Not recorded Small vasohibin-binding protein × 1 (Q8N300) M4Y parthenolide × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;0.2 M ammonium sulfate, 0.1 M Bis-tris, pH 5.5, and 25 % (w/v) PEG 3350 Resolution 2.00 Å R-free 0.229

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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VASH1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–242; UniProt 61–302 Author chain C; PDBConstruct 1–242; UniProt 61–302

Small vasohibin-binding protein

Homo sapiens

UniProt Q8N300

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 25–52 Not recorded Tubulinyl-Tyr carboxypeptidase 1 × 1 (Q7L8A9) M4Y parthenolide × 1 GOL GLYCEROL × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;0.2 M ammonium sulfate, 0.1 M Bis-tris, pH 5.5, and 25 % (w/v) PEG 3350 Resolution 2.00 Å R-free 0.229
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 25–52 Not recorded Tubulinyl-Tyr carboxypeptidase 1 × 1 (Q7L8A9) M4Y parthenolide × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;0.2 M ammonium sulfate, 0.1 M Bis-tris, pH 5.5, and 25 % (w/v) PEG 3350 Resolution 2.00 Å R-free 0.229

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.

23 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SVBP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–28; UniProt 25–52 Author chain D; PDBConstruct 1–28; UniProt 25–52

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 6och

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6och
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6och
Deposition date deposition_date2019-03-23
Structure title titleCrystal structure of VASH1-SVBP complex bound with parthenolide
Keywords keywordstubulin carboxypeptidases, VASH1-SVBP complex, Parthenolide, microtubule detyrosination, hydrolase-hydrolase inhibitor complex; hydrolase/hydrolase inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.10
Radius of gyration Rg (electron density) rg_electron29.27
Forward intensity I(0) i065613600.00
Molecular weight molecular_weight63570.0 kDa
Excluded volume excluded_volume79678 ų
Envelope volume envelope_volume99868 ų
Hydration-shell volume shell_volume29503 ų
Envelope diameter envelope_diameter97.7
Shell Rg shell_rg35.24
Envelope Rg envelope_rg29.35
Shape Rg shape_rg29.28
Total Rg total_rg29.85
Total atoms total_atoms4511
Residues n_residues539
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 dmax97.1
Rg (real space) rg_real30.16
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real6.5610e+07
I(0) uncertainty (real space) i0_real_error9.5820e+05
Rg (reciprocal space) rg_reciprocal30.14
I(0) (reciprocal space) i0_reciprocal65610000.0000
Solution quality estimate total_estimate0.8919
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.317
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23140000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.933; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)