8b8i

Nanobody (NbLumSyt1) bound to human Syt1

Method: X-RAY DIFFRACTION Dmax: 92.9 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 I; UniProt 1–60 Not recorded Nanobody (NbLumSyt1) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1.6 M DL-malic acid Resolution 2.75 Å R-free 0.298
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain J; UniProt 1–60 Not recorded Nanobody (NbLumSyt1) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1.6 M DL-malic acid Resolution 2.75 Å R-free 0.298
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 1–60 Not recorded Nanobody (NbLumSyt1) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1.6 M DL-malic acid Resolution 2.75 Å R-free 0.298
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain L; UniProt 1–60 Not recorded Nanobody (NbLumSyt1) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1.6 M DL-malic acid Resolution 2.75 Å R-free 0.298
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain M; UniProt 1–60 Not recorded Nanobody (NbLumSyt1) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1.6 M DL-malic acid Resolution 2.75 Å R-free 0.298
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain N; UniProt 1–60 Not recorded Nanobody (NbLumSyt1) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1.6 M DL-malic acid Resolution 2.75 Å R-free 0.298
7 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain O; UniProt 1–60 Not recorded Nanobody (NbLumSyt1) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1.6 M DL-malic acid Resolution 2.75 Å R-free 0.298
8 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain P; UniProt 1–60 Not recorded Nanobody (NbLumSyt1) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1.6 M DL-malic acid Resolution 2.75 Å R-free 0.298

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYT1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–60; UniProt 1–60 Author chain J; PDBConstruct 1–60; UniProt 1–60 Author chain K; PDBConstruct 1–60; UniProt 1–60 Author chain L; PDBConstruct 1–60; UniProt 1–60 Author chain M; PDBConstruct 1–60; UniProt 1–60 Author chain N; PDBConstruct 1–60; UniProt 1–60 Author chain O; PDBConstruct 1–60; UniProt 1–60 Author chain P; PDBConstruct 1–60; UniProt 1–60

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 8b8i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8b8i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8b8i
Deposition date deposition_date2022-10-04
Structure title titleNanobody (NbLumSyt1) bound to human Syt1
Keywords keywordsSyt1, nanobody, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.72
Radius of gyration Rg (electron density) rg_electron29.62
Forward intensity I(0) i0208660000.00
Molecular weight molecular_weight109760.0 kDa
Excluded volume excluded_volume134870 ų
Envelope volume envelope_volume168370 ų
Hydration-shell volume shell_volume46037 ų
Envelope diameter envelope_diameter99.5
Shell Rg shell_rg37.88
Envelope Rg envelope_rg29.66
Shape Rg shape_rg29.65
Total Rg total_rg30.18
Total atoms total_atoms7705
Residues n_residues1052
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 dmax92.9
Rg (real space) rg_real30.53
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real2.0870e+08
I(0) uncertainty (real space) i0_real_error2.5460e+06
Rg (reciprocal space) rg_reciprocal30.61
I(0) (reciprocal space) i0_reciprocal208700000.0000
Solution quality estimate total_estimate0.8884
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.1
Skewness Skewness skewness0.170
Kurtosis Kurtosis kurtosis-0.310
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86310000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)