4b1x

Structure of the Phactr1 RPEL-2 bound to G-actin

Method: X-RAY DIFFRACTION Dmax: 73.2 Å Quality: GOOD

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

ACTIN, ALPHA SKELETAL MUSCLE

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 B; UniProt 2–377 Not recorded PHOSPHATASE AND ACTIN REGULATOR 1 × 1 (G5E8P7) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.80 Å R-free 0.213

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 B; PDBConstruct 1–376; UniProt 2–377

PHOSPHATASE AND ACTIN REGULATOR 1

OrganismNot specified

UniProt G5E8P7

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 M; UniProt 524–555 Fragment:RESIDUES 524-555 ACTIN, ALPHA SKELETAL MUSCLE × 1 (P68135) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.80 Å R-free 0.213

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G5E8P7_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 1–32; UniProt 524–555

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 4b1x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4b1x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4b1x
Deposition date deposition_date2012-07-12
Structure title titleStructure of the Phactr1 RPEL-2 bound to G-actin
Keywords keywordsSTRUCTURAL PROTEIN, NUCLEOTIDE-BINDING, TRANSCRIPTION REGULATION, TRANSCRIPTION, MUSCLE PROTEIN, ATP-BINDING, CYTOSKELETON; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.35
Radius of gyration Rg (electron density) rg_electron21.40
Forward intensity I(0) i032785200.00
Molecular weight molecular_weight43569.0 kDa
Excluded volume excluded_volume54310 ų
Envelope volume envelope_volume62575 ų
Hydration-shell volume shell_volume24115 ų
Envelope diameter envelope_diameter75.4
Shell Rg shell_rg28.40
Envelope Rg envelope_rg21.77
Shape Rg shape_rg21.42
Total Rg total_rg22.16
Total atoms total_atoms3054
Residues n_residues385
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 dmax73.2
Rg (real space) rg_real22.29
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real3.2790e+07
I(0) uncertainty (real space) i0_real_error4.5650e+05
Rg (reciprocal space) rg_reciprocal22.31
I(0) (reciprocal space) i0_reciprocal32790000.0000
Solution quality estimate total_estimate0.8900
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.6
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.380
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9047000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id4b1xB01
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_id4b1xB02
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_id4b1xB03
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)