6ocf

The crystal structure of VASH1-SVBP complex

Method: X-RAY DIFFRACTION Dmax: 85.2 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 58–305 Non-standard monomer:Yes (specific site not provided by mmCIF) Small vasohibin-binding protein × 1 (Q8N300) GOL GLYCEROL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;293.15 K;0.1 M sodium citrate tribasic dihydrate, pH 5.0, and 18% (w/v) PEG20000 Resolution 2.10 Å R-free 0.222

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 1–248; UniProt 58–305

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 18–66 Non-standard monomer:Yes (specific site not provided by mmCIF) Tubulinyl-Tyr carboxypeptidase 1 × 1 (Q7L8A9) GOL GLYCEROL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;293.15 K;0.1 M sodium citrate tribasic dihydrate, pH 5.0, and 18% (w/v) PEG20000 Resolution 2.10 Å R-free 0.222

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 1–49; UniProt 18–66

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 6ocf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ocf
Deposition date deposition_date2019-03-23
Structure title titleThe crystal structure of VASH1-SVBP complex
Keywords keywordstubulin carboxypeptidases, microtubule modification, tubulin detyrosination, VASH1-SVBP complex, HYDROLASE-PROTEIN BINDING complex; HYDROLASE/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.28
Radius of gyration Rg (electron density) rg_electron21.23
Forward intensity I(0) i021665500.00
Molecular weight molecular_weight35164.0 kDa
Excluded volume excluded_volume43807 ų
Envelope volume envelope_volume54802 ų
Hydration-shell volume shell_volume21649 ų
Envelope diameter envelope_diameter87.9
Shell Rg shell_rg27.69
Envelope Rg envelope_rg22.06
Shape Rg shape_rg21.26
Total Rg total_rg22.00
Total atoms total_atoms2453
Residues n_residues288
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 dmax85.2
Rg (real space) rg_real22.26
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real2.1670e+07
I(0) uncertainty (real space) i0_real_error3.2920e+05
Rg (reciprocal space) rg_reciprocal22.27
I(0) (reciprocal space) i0_reciprocal21670000.0000
Solution quality estimate total_estimate0.8190
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.5
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.210
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4036000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.587; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.886; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)