6j8f

Crystal structure of SVBP-VASH1 with peptide mimic the C-terminal of alpha-tubulin

Method: X-RAY DIFFRACTION Dmax: 68.3 Å Quality: GOOD

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 3–48 Not recorded Tubulinyl-Tyr carboxypeptidase 1 × 1 (Q7L8A9) 8-mer peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M Na citrate tribasic dihydrate pH 5.0, 18% PEG 20000 Resolution 2.28 Å R-free 0.237

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–46; UniProt 3–48

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 70–306 Not recorded Small vasohibin-binding protein × 1 (Q8N300) 8-mer peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M Na citrate tribasic dihydrate pH 5.0, 18% PEG 20000 Resolution 2.28 Å R-free 0.237

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 2
Chains and sequence ranges Author chain B; PDBConstruct 2–238; UniProt 70–306

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 6j8f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6j8f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6j8f
Deposition date deposition_date2019-01-18
Structure title titleCrystal structure of SVBP-VASH1 with peptide mimic the C-terminal of alpha-tubulin
Keywords keywords;protease, complex, PEPTIDE BINDING PROTEIN, Structural Genomics, PSI-2, Protein Structure Initiative, Structural Genomics Consortium, SGC, PEPTIDE BINDING PROTEIN-HYDROLASE complex ;; PEPTIDE BINDING PROTEIN/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.86
Radius of gyration Rg (electron density) rg_electron19.68
Forward intensity I(0) i016031300.00
Molecular weight molecular_weight30398.0 kDa
Excluded volume excluded_volume38178 ų
Envelope volume envelope_volume45789 ų
Hydration-shell volume shell_volume19652 ų
Envelope diameter envelope_diameter68.7
Shell Rg shell_rg25.81
Envelope Rg envelope_rg20.07
Shape Rg shape_rg19.68
Total Rg total_rg20.54
Total atoms total_atoms2141
Residues n_residues261
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 dmax68.3
Rg (real space) rg_real20.83
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.6030e+07
I(0) uncertainty (real space) i0_real_error2.1450e+05
Rg (reciprocal space) rg_reciprocal20.84
I(0) (reciprocal space) i0_reciprocal16030000.0000
Solution quality estimate total_estimate0.8915
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.319
Kurtosis Kurtosis kurtosis-0.334
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3362000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)