5lob

Structure of the Ca2+-bound Rabphilin3A C2B- SNAP25 complex (C2 space group)

Method: X-RAY DIFFRACTION Dmax: 165.8 Å Quality: REASONABLE

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

Rabphilin-3A

Rattus norvegicus

UniProt P47709

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 536–680 Chain B; UniProt 536–680 Chain C; UniProt 536–680 Not recorded Synaptosomal-associated protein 25 × 2 (P60881) Synaptosomal-associated protein 25 × 2 (P60881) CA CALCIUM ION × 6 SO4 SULFATE ION × 10 GOL GLYCEROL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;30% PEG3350 0.35 M Ammonium sulfate 0.1 M Tris pH 8.5 Resolution 3.30 Å R-free 0.286

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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RP3A_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 18–162; UniProt 536–680 Author chain B; PDBConstruct 18–162; UniProt 536–680 Author chain C; PDBConstruct 18–162; UniProt 536–680

Synaptosomal-associated protein 25

Rattus norvegicus

UniProt P60881

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 7–82 Chain E; UniProt 141–203 Chain F; UniProt 7–82 Chain G; UniProt 141–203 Fragment:N-terminal helix Fragment:C-terminal helix Rabphilin-3A × 3 (P47709) CA CALCIUM ION × 6 SO4 SULFATE ION × 10 GOL GLYCEROL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;30% PEG3350 0.35 M Ammonium sulfate 0.1 M Tris pH 8.5 Resolution 3.30 Å R-free 0.286

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.

39 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNP25_RAT
Isoform P60881-2
PDB entities 2, 3
Chains and sequence ranges Author chain D; PDBConstruct 25–100; UniProt 7–82 Author chain F; PDBConstruct 25–100; UniProt 7–82 Author chain E; PDBConstruct 34–96; UniProt 141–203 Author chain G; PDBConstruct 34–96; UniProt 141–203

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 5lob

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5lob
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5lob
Deposition date deposition_date2016-08-09
Structure title titleStructure of the Ca2+-bound Rabphilin3A C2B- SNAP25 complex (C2 space group)
Keywords keywordsmembrane fusion, SNARE complex, PIP2, C2 domain, Exocytosis; EXOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.77
Radius of gyration Rg (electron density) rg_electron41.43
Forward intensity I(0) i0124883000.00
Molecular weight molecular_weight85030.0 kDa
Excluded volume excluded_volume104550 ų
Envelope volume envelope_volume156100 ų
Hydration-shell volume shell_volume36090 ų
Envelope diameter envelope_diameter173.9
Shell Rg shell_rg39.36
Envelope Rg envelope_rg43.21
Shape Rg shape_rg41.41
Total Rg total_rg41.34
Total atoms total_atoms5922
Residues n_residues725
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 dmax165.8
Rg (real space) rg_real41.42
Rg uncertainty (real space) rg_real_error2.31
I(0) (real space) i0_real1.2490e+08
I(0) uncertainty (real space) i0_real_error2.5220e+06
Rg (reciprocal space) rg_reciprocal40.77
I(0) (reciprocal space) i0_reciprocal124800000.0000
Solution quality estimate total_estimate0.7104
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.5
Skewness Skewness skewness0.795
Kurtosis Kurtosis kurtosis0.472
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6537000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.383; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.195; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5lobA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily150 — C2 domain
Domain ID domain_id5lobB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily150 — C2 domain
Domain ID domain_id5lobC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily150 — C2 domain
Domain ID domain_id5lobE00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily110

8. Citations (1)

9. Files and Curves (10)