1k5w

THREE-DIMENSIONAL STRUCTURE OF THE SYNAPTOTAGMIN 1 C2B-DOMAIN: SYNAPTOTAGMIN 1 AS A PHOSPHOLIPID BINDING MACHINE

Method: SOLUTION NMR Dmax: 49.1 Å Quality: GOOD

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

Synaptotagmin I

Rattus norvegicus

UniProt P21707

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 270–421 Fragment:Residues 270-421, C2B-Domain CA CALCIUM ION × 2 SOLUTION NMR NMR measurement conditions:pH 6.3;303 K;Ionic strength (raw mmCIF value) 150mM NaCl;Pressure 1 NMR sample composition:0.0013M 15N, 13C C2B-Domain | 50mM Mes 2mM DTT 20mM CaCl2 5%D2O NMR sample composition:1.3mM 15N, C2B-Domain | 50mM Mes 2mM DTT 20mM CaCl2 5%D2O NMR sample composition:0.4mM 15N, C2B-Domain | 50mM Mes 2mM DTT 0.5mM EDTA 5%D2O NMR sample composition:1mM 10% 13C, C2B-Domain | 50mM Mes 2mM DTT 20mM CaCl2 5%D2O Resolution not provided

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.

19 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYT1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–152; UniProt 270–421

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 1k5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k5w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k5w
Deposition date deposition_date2001-10-12
Structure title titleTHREE-DIMENSIONAL STRUCTURE OF THE SYNAPTOTAGMIN 1 C2B-DOMAIN: SYNAPTOTAGMIN 1 AS A PHOSPHOLIPID BINDING MACHINE
Keywords keywords;C2B-DOMAIN, C2-DOMAIN, SYNAPTOTAGMIN I, CALCIUM-BINDING, PHOSPHOLIPID-BINDING, SYNAPSIS, NEUROTRANSMITTER RELEASE, SYNAPTIC VESICLE EXOCYTOSIS, ENDOCYTOSIS-EXOCYTOSIS COMPLEX ;; ENDOCYTOSIS/EXOCYTOSIS
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.12
Radius of gyration Rg (electron density) rg_electron15.02
Forward intensity I(0) i01411160000.00
Molecular weight molecular_weight337620.0 kDa
Excluded volume excluded_volume430160 ų
Envelope volume envelope_volume29959 ų
Hydration-shell volume shell_volume15589 ų
Envelope diameter envelope_diameter55.5
Shell Rg shell_rg22.27
Envelope Rg envelope_rg16.56
Shape Rg shape_rg14.97
Total Rg total_rg15.30
Total atoms total_atoms48200
Residues n_residues2960
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 dmax49.1
Rg (real space) rg_real15.09
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.4110e+09
I(0) uncertainty (real space) i0_real_error1.5160e+07
Rg (reciprocal space) rg_reciprocal15.09
I(0) (reciprocal space) i0_reciprocal1411000000.0000
Solution quality estimate total_estimate0.8111
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.0
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha460000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1k5wa_
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.1 — C2 domain (Calcium/lipid-binding domain, CaLB)
Family Family familyb.7.1.2 — Synaptotagmin-like (S variant)

CATH v4.4 (1 domains)

Domain ID domain_id1k5wA00
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)