4h0t

Crystal structure of Ia-ADPR-actin complex

Method: X-RAY DIFFRACTION Dmax: 102.3 Å Quality: GOOD

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

Iota toxin component Ia

Clostridium perfringens

UniProt Q46220

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 42–454 Not recorded Actin, alpha skeletal muscle × 1 (P68135) PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 18 AR6 [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE × 1 CA CALCIUM ION × 1 LAR LATRUNCULIN A × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.13 K;18% PEG1500, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.13K Resolution 2.20 Å R-free 0.240

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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q46220_CLOPF
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–418; UniProt 42–454

Actin, alpha skeletal muscle

Oryctolagus cuniculus

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 B; UniProt 3–377 Not recorded Iota toxin component Ia × 1 (Q46220) PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 18 AR6 [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE × 1 CA CALCIUM ION × 1 LAR LATRUNCULIN A × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277.13 K;18% PEG1500, 0.1M MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.13K Resolution 2.20 Å R-free 0.240

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 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–375; UniProt 3–377

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 4h0t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4h0t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4h0t
Deposition date deposition_date2012-09-10
Structure title titleCrystal structure of Ia-ADPR-actin complex
Keywords keywordsADP-ribosyltransferase, TOXIN-STRUCTURAL PROTEIN complex; TOXIN/STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.97
Radius of gyration Rg (electron density) rg_electron30.52
Forward intensity I(0) i0127567000.00
Molecular weight molecular_weight90295.0 kDa
Excluded volume excluded_volume113150 ų
Envelope volume envelope_volume138980 ų
Hydration-shell volume shell_volume38442 ų
Envelope diameter envelope_diameter110.0
Shell Rg shell_rg37.27
Envelope Rg envelope_rg30.71
Shape Rg shape_rg30.52
Total Rg total_rg31.07
Total atoms total_atoms6343
Residues n_residues772
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 dmax102.3
Rg (real space) rg_real31.04
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real1.2760e+08
I(0) uncertainty (real space) i0_real_error1.8560e+06
Rg (reciprocal space) rg_reciprocal31.02
I(0) (reciprocal space) i0_reciprocal127600000.0000
Solution quality estimate total_estimate0.8801
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.1
Skewness Skewness skewness0.430
Kurtosis Kurtosis kurtosis-0.291
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23960000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.915

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd4h0ta1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.166 — ADP-ribosylation
Superfamily Superfamily superfamilyd.166.1 — ADP-ribosylation
Family Family familyd.166.1.1 — ADP-ribosylating toxins
Domain ID domain_idd4h0ta2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.166 — ADP-ribosylation
Superfamily Superfamily superfamilyd.166.1 — ADP-ribosylation
Family Family familyd.166.1.1 — ADP-ribosylating toxins
Domain ID domain_idd4h0ta3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4h0tb1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd4h0tb2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70

CATH v4.4 (5 domains)

Domain ID domain_id4h0tA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology176 — Toxin ADP-ribosyltransferase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Toxin ADP-ribosyltransferase; Chain A, domain 1
Domain ID domain_id4h0tA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology176 — Toxin ADP-ribosyltransferase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Toxin ADP-ribosyltransferase; Chain A, domain 1
Domain ID domain_id4h0tB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id4h0tB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id4h0tB03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4

8. Citations (1)

9. Files and Curves (10)