1rdw

Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer

Method: X-RAY DIFFRACTION Dmax: 73.1 Å Quality: GOOD

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

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain X; UniProt 3–377 Fragment:ACtin MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 LAR LATRUNCULIN A × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;MgCl2, NH4SO4, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.30 Å R-free 0.224

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 X; 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 1rdw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rdw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rdw
Deposition date deposition_date2003-11-06
Structure title titleActin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer
Keywords keywordsAnti-parallel dimer, Polymerization, Nucleation, Filament, 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_guinier22.15
Radius of gyration Rg (electron density) rg_electron21.27
Forward intensity I(0) i029317900.00
Molecular weight molecular_weight41262.0 kDa
Excluded volume excluded_volume51467 ų
Envelope volume envelope_volume60014 ų
Hydration-shell volume shell_volume23398 ų
Envelope diameter envelope_diameter75.6
Shell Rg shell_rg28.08
Envelope Rg envelope_rg21.64
Shape Rg shape_rg21.30
Total Rg total_rg22.03
Total atoms total_atoms2891
Residues n_residues361
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 dmax73.1
Rg (real space) rg_real22.10
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real2.9320e+07
I(0) uncertainty (real space) i0_real_error3.9440e+05
Rg (reciprocal space) rg_reciprocal22.11
I(0) (reciprocal space) i0_reciprocal29320000.0000
Solution quality estimate total_estimate0.8094
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.303
Kurtosis Kurtosis kurtosis-0.361
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9069000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1rdwx1
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_idd1rdwx2
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 (4 domains)

Domain ID domain_id1rdwX01
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_id1rdwX02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology36 — Actin; Chain A, domain 2
Homologous superfamily homologous superfamily70 — Actin; Chain A, domain 2
Domain ID domain_id1rdwX03
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_id1rdwX04
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)