4h03

Crystal structure of NAD+-Ia-actin complex

Method: X-RAY DIFFRACTION Dmax: 104.0 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) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 48 CA CALCIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 LAR LATRUNCULIN A × 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 1.75 Å R-free 0.233

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 Non-standard monomer:Yes (specific site not provided by mmCIF) Iota toxin component Ia × 1 (Q46220) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 PO4 PHOSPHATE ION × 1 EDO 1,2-ETHANEDIOL × 48 CA CALCIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 LAR LATRUNCULIN A × 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 1.75 Å R-free 0.233

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 4h03

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4h03
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4h03
Deposition date deposition_date2012-09-07
Structure title titleCrystal structure of NAD+-Ia-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_guinier31.03
Radius of gyration Rg (electron density) rg_electron30.61
Forward intensity I(0) i0133097000.00
Molecular weight molecular_weight92293.0 kDa
Excluded volume excluded_volume115770 ų
Envelope volume envelope_volume141110 ų
Hydration-shell volume shell_volume38875 ų
Envelope diameter envelope_diameter110.8
Shell Rg shell_rg37.26
Envelope Rg envelope_rg30.79
Shape Rg shape_rg30.61
Total Rg total_rg31.14
Total atoms total_atoms6473
Residues n_residues771
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 dmax104.0
Rg (real space) rg_real31.10
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real1.3310e+08
I(0) uncertainty (real space) i0_real_error2.0410e+06
Rg (reciprocal space) rg_reciprocal31.08
I(0) (reciprocal space) i0_reciprocal133100000.0000
Solution quality estimate total_estimate0.8759
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.7
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.269
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26570000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.943

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_idd4h03a1
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_idd4h03a2
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_idd4h03a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4h03b1
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_idd4h03b2
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_id4h03A01
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_id4h03A02
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_id4h03B01
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_id4h03B02
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_id4h03B03
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)