6j4u

Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications

Method: X-RAY DIFFRACTION Dmax: 70.3 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 57–307 Mutation:E71S/A72H/K79M Small vasohibin-binding protein × 1 (Q8N300) X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 5;293 K;by introducing three mutations E71S/A72H/K79M into V1c allowed us to solve the V1c-SVBP to high resolution. Well diffracting crystals of the mutant V1c-SVBP complex were obtained in 1.0 M lithium chloride, 0.1 M citric acid, pH 5.0, 20% PEG 6000. Resolution 2.00 Å R-free 0.204

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 16 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 1–251; UniProt 57–307

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 1–66 Not recorded Tubulinyl-Tyr carboxypeptidase 1 × 1 (Q7L8A9) X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 5;293 K;by introducing three mutations E71S/A72H/K79M into V1c allowed us to solve the V1c-SVBP to high resolution. Well diffracting crystals of the mutant V1c-SVBP complex were obtained in 1.0 M lithium chloride, 0.1 M citric acid, pH 5.0, 20% PEG 6000. Resolution 2.00 Å R-free 0.204

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 31 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 1–66; UniProt 1–66

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 6j4u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6j4u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6j4u
Deposition date deposition_date2019-01-10
Structure title titleStructural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and functional implications
Keywords keywordscarboxypeptidase, tubulin, microtubule., HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.17
Radius of gyration Rg (electron density) rg_electron19.89
Forward intensity I(0) i017639600.00
Molecular weight molecular_weight31904.0 kDa
Excluded volume excluded_volume40095 ų
Envelope volume envelope_volume47889 ų
Hydration-shell volume shell_volume20202 ų
Envelope diameter envelope_diameter70.3
Shell Rg shell_rg26.29
Envelope Rg envelope_rg20.18
Shape Rg shape_rg19.89
Total Rg total_rg20.81
Total atoms total_atoms2248
Residues n_residues276
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 dmax70.3
Rg (real space) rg_real21.12
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.7640e+07
I(0) uncertainty (real space) i0_real_error2.1080e+05
Rg (reciprocal space) rg_reciprocal21.13
I(0) (reciprocal space) i0_reciprocal17640000.0000
Solution quality estimate total_estimate0.8893
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.280
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3692000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)