8br1

ExoY Nucleotidyl Cyclase domain from Vibrio nigripulchritudo MARTX toxin, bound to Latrunculin-B-ATP-Mg-actin, and 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE and 2 Mg ions

Method: X-RAY DIFFRACTION Dmax: 141.3 Å Quality: GOOD

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

Actin, alpha skeletal muscle, intermediate form

OrganismNot specified

UniProt P68135

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 3–377 Not recorded Putative Adenylate cyclase × 1 (A0A6N3LUE9) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 3 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE × 1 SO4 SULFATE ION × 1 GOL GLYCEROL × 1 PEO HYDROGEN PEROXIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;26 % peg 3350, 26 % Glycerol, 30 mM LiSO4, 0.1M TrisHCl pH8.5, 3 % Dioxane, Resolution 2.04 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 3–377 Not recorded Putative Adenylate cyclase × 1 (A0A6N3LUE9) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 3 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;26 % peg 3350, 26 % Glycerol, 30 mM LiSO4, 0.1M TrisHCl pH8.5, 3 % Dioxane, Resolution 2.04 Å R-free 0.222

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.

293 other PDB entries and 352 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–375; UniProt 3–377 Author chain C; PDBConstruct 1–375; UniProt 3–377

Putative Adenylate cyclase

Vibrio nigripulchritudo

UniProt A0A6N3LUE9

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 3455–3863 Not recorded Actin, alpha skeletal muscle, intermediate form × 1 (P68135) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 3 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE × 1 SO4 SULFATE ION × 1 GOL GLYCEROL × 1 PEO HYDROGEN PEROXIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;26 % peg 3350, 26 % Glycerol, 30 mM LiSO4, 0.1M TrisHCl pH8.5, 3 % Dioxane, Resolution 2.04 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 3455–3863 Not recorded Actin, alpha skeletal muscle, intermediate form × 1 (P68135) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 3 3AT 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;26 % peg 3350, 26 % Glycerol, 30 mM LiSO4, 0.1M TrisHCl pH8.5, 3 % Dioxane, Resolution 2.04 Å R-free 0.222

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.

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6N3LUE9_9VIBR
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–413; UniProt 3455–3863 Author chain D; PDBConstruct 5–413; UniProt 3455–3863

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 8br1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8br1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8br1
Deposition date deposition_date2022-11-22
Structure title titleExoY Nucleotidyl Cyclase domain from Vibrio nigripulchritudo MARTX toxin, bound to Latrunculin-B-ATP-Mg-actin, and 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE and 2 Mg ions
Keywords keywordsbacterial nucleotidyl cyclase toxin, activated complex, TOXIN; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.17
Radius of gyration Rg (electron density) rg_electron42.06
Forward intensity I(0) i0456914000.00
Molecular weight molecular_weight173080.0 kDa
Excluded volume excluded_volume215520 ų
Envelope volume envelope_volume290910 ų
Hydration-shell volume shell_volume58291 ų
Envelope diameter envelope_diameter146.1
Shell Rg shell_rg46.76
Envelope Rg envelope_rg41.29
Shape Rg shape_rg42.08
Total Rg total_rg42.23
Total atoms total_atoms12156
Residues n_residues1518
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 dmax141.3
Rg (real space) rg_real42.22
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real4.5690e+08
I(0) uncertainty (real space) i0_real_error8.3660e+06
Rg (reciprocal space) rg_reciprocal42.18
I(0) (reciprocal space) i0_reciprocal456900000.0000
Solution quality estimate total_estimate0.8857
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.8
Skewness Skewness skewness0.310
Kurtosis Kurtosis kurtosis-0.510
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49670000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.844

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)