2q0r

Structure of Pectenotoxin-2 Bound to Actin

Method: X-RAY DIFFRACTION Dmax: 71.7 Å Quality: GOOD

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

Actin

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 3–377 Not recorded CA CALCIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 PXT PECTENOTOXIN-2 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;100 mM Na/MES/acetate, pH 5.5, 15% methyl ether poly(ethylene glycol) 5000, 10% hexanediol, 30 mM CaCl2, and 1 mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.70 Å R-free 0.204

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 1
Chains and sequence ranges Author chain A; 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 2q0r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2q0r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2q0r
Deposition date deposition_date2007-05-22
Structure title titleStructure of Pectenotoxin-2 Bound to Actin
Keywords keywordspectenotoxin, actin, anti-tumor, filament capping, natural product, cytotoxin, macrolide, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.00
Radius of gyration Rg (electron density) rg_electron21.06
Forward intensity I(0) i027748100.00
Molecular weight molecular_weight40659.0 kDa
Excluded volume excluded_volume50933 ų
Envelope volume envelope_volume58359 ų
Hydration-shell volume shell_volume23007 ų
Envelope diameter envelope_diameter75.7
Shell Rg shell_rg27.95
Envelope Rg envelope_rg21.46
Shape Rg shape_rg21.09
Total Rg total_rg21.86
Total atoms total_atoms2847
Residues n_residues360
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 dmax71.7
Rg (real space) rg_real21.95
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real2.7750e+07
I(0) uncertainty (real space) i0_real_error3.6400e+05
Rg (reciprocal space) rg_reciprocal21.96
I(0) (reciprocal space) i0_reciprocal27750000.0000
Solution quality estimate total_estimate0.8131
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.7
Skewness Skewness skewness0.298
Kurtosis Kurtosis kurtosis-0.370
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8189000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2q0ra1
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_idd2q0ra2
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 (3 domains)

Domain ID domain_id2q0rA01
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_id2q0rA02
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_id2q0rA03
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)