4v11

Structure of Synaptotagmin-1 with SV2A peptide phosphorylated at Thr84

Method: X-RAY DIFFRACTION Dmax: 54.2 Å Quality: GOOD

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

SYNAPTOTAGMIN-1

HOMO SAPIENS

UniProt P21579

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 273–422 Fragment:C2B DOMAIN, UNP RESIDUES 273-422 SYNAPTIC VESICLE GLYCOPROTEIN 2A × 1 (Q7L0J3) CA CALCIUM ION × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1 M HEPES PH 7.5, 18 % PEG 3350, 0.05 M CACL2 Resolution 1.95 Å R-free 0.196

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.

21 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–150; UniProt 273–422

SYNAPTIC VESICLE GLYCOPROTEIN 2A

OrganismNot specified

UniProt Q7L0J3

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 81–90 Fragment:UNP RESIDUES 81-90 Non-standard monomer:Yes (specific site not provided by mmCIF) SYNAPTOTAGMIN-1 × 1 (P21579) CA CALCIUM ION × 3 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1 M HEPES PH 7.5, 18 % PEG 3350, 0.05 M CACL2 Resolution 1.95 Å R-free 0.196

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SV2A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 81–90

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 4v11

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4v11
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4v11
Deposition date deposition_date2014-09-22
Structure title titleStructure of Synaptotagmin-1 with SV2A peptide phosphorylated at Thr84
Keywords keywordsSIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.56
Radius of gyration Rg (electron density) rg_electron15.37
Forward intensity I(0) i06299580.00
Molecular weight molecular_weight18439.0 kDa
Excluded volume excluded_volume23264 ų
Envelope volume envelope_volume26374 ų
Hydration-shell volume shell_volume14448 ų
Envelope diameter envelope_diameter55.4
Shell Rg shell_rg21.34
Envelope Rg envelope_rg15.81
Shape Rg shape_rg15.32
Total Rg total_rg16.64
Total atoms total_atoms1290
Residues n_residues159
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 dmax54.2
Rg (real space) rg_real16.46
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real6.3000e+06
I(0) uncertainty (real space) i0_real_error8.2710e+04
Rg (reciprocal space) rg_reciprocal16.47
I(0) (reciprocal space) i0_reciprocal6300000.0000
Solution quality estimate total_estimate0.7954
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.195
Kurtosis Kurtosis kurtosis-0.228
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1375000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4v11A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily150 — C2 domain

8. Citations (1)

9. Files and Curves (10)