4b1y

Structure of the Phactr1 RPEL-3 bound to G-actin

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

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 1PE PENTAETHYLENE GLYCOL × 1 GOL GLYCEROL × 1 PEG DI(HYDROXYETHYL)ETHER × 3 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.29 Å R-free 0.174

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

MUS MUSCULUS

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 562–593 Fragment:RESIDUES 562-593 ACTIN, ALPHA SKELETAL MUSCLE × 1 (P68135) LAB LATRUNCULIN B × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 1PE PENTAETHYLENE GLYCOL × 1 GOL GLYCEROL × 1 PEG DI(HYDROXYETHYL)ETHER × 3 P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.29 Å R-free 0.174

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 562–593

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 4b1y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4b1y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4b1y
Deposition date deposition_date2012-07-12
Structure title titleStructure of the Phactr1 RPEL-3 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_guinier22.55
Radius of gyration Rg (electron density) rg_electron21.61
Forward intensity I(0) i035713000.00
Molecular weight molecular_weight45954.0 kDa
Excluded volume excluded_volume57481 ų
Envelope volume envelope_volume65979 ų
Hydration-shell volume shell_volume25026 ų
Envelope diameter envelope_diameter73.5
Shell Rg shell_rg28.82
Envelope Rg envelope_rg21.96
Shape Rg shape_rg21.63
Total Rg total_rg22.40
Total atoms total_atoms3218
Residues n_residues394
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_real22.47
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real3.5710e+07
I(0) uncertainty (real space) i0_real_error4.4020e+05
Rg (reciprocal space) rg_reciprocal22.49
I(0) (reciprocal space) i0_reciprocal35710000.0000
Solution quality estimate total_estimate0.9020
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.1
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.445
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9624000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4b1yb1
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.55.1.0 — automated matches
Domain ID domain_idd4b1yb2
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_id4b1yB01
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_id4b1yB02
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_id4b1yB03
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)