4j2q

Crystal structure of C-terminally truncated arrestin reveals mechanism of arrestin activation

Method: X-RAY DIFFRACTION Dmax: 112.5 Å Quality: GOOD

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

S-arrestin

Bos taurus

UniProt P08168

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 A; UniProt 1–369 Chain B; UniProt 1–369 Fragment:UNP residues 1-369 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;30% polyethylene glycol 200, 10 mM HEPES, 100 mM lithium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.00 Å R-free 0.279

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.

16 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARRS_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–379; UniProt 1–369 Author chain B; PDBConstruct 11–379; UniProt 1–369

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 4j2q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4j2q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4j2q
Deposition date deposition_date2013-02-05
Structure title titleCrystal structure of C-terminally truncated arrestin reveals mechanism of arrestin activation
Keywords keywords;ARRESTIN FOLD, SIGNAL TERMINATION, GPCR, OUTER SEGMENT, SIGNALING PROTEIN, P44, RHODOPSIN, G-PROTEIN, SPLICE VARIANT MUTANT ARRESTIN, S-ANTIGEN, DEACTIVATION, VISUAL SIGNAL TRANSDUCTION ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.86
Radius of gyration Rg (electron density) rg_electron33.69
Forward intensity I(0) i085371800.00
Molecular weight molecular_weight76539.0 kDa
Excluded volume excluded_volume97451 ų
Envelope volume envelope_volume134460 ų
Hydration-shell volume shell_volume34781 ų
Envelope diameter envelope_diameter119.4
Shell Rg shell_rg38.17
Envelope Rg envelope_rg33.81
Shape Rg shape_rg33.67
Total Rg total_rg34.16
Total atoms total_atoms5390
Residues n_residues686
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 dmax112.5
Rg (real space) rg_real33.96
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real8.5370e+07
I(0) uncertainty (real space) i0_real_error1.5130e+06
Rg (reciprocal space) rg_reciprocal33.90
I(0) (reciprocal space) i0_reciprocal85370000.0000
Solution quality estimate total_estimate0.8739
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary110.1
Skewness Skewness skewness0.362
Kurtosis Kurtosis kurtosis-0.528
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18410000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.859; Smooth: 0.839

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4j2qa1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.11 — Arrestin/Vps26-like
Domain ID domain_idd4j2qa2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.11 — Arrestin/Vps26-like
Domain ID domain_idd4j2qb1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.11 — Arrestin/Vps26-like
Domain ID domain_idd4j2qb2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.11 — Arrestin/Vps26-like

CATH v4.4 (4 domains)

Domain ID domain_id4j2qA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily840
Domain ID domain_id4j2qA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily640
Domain ID domain_id4j2qB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily840
Domain ID domain_id4j2qB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily640

8. Citations (1)

9. Files and Curves (10)