8i10

Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Vasopressin V2 receptor, V2R (Local refine)

Method: ELECTRON MICROSCOPY Dmax: 142.4 Å Quality: GOOD

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

Beta-arrestin-2

Bos taurus

UniProt P32120

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–420 Chain B; UniProt 1–420 Chain C; UniProt 1–420 Mutation:C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Fab30 Heavy Chain × 3 Fab30 Light Chain × 3 Vasopressin V2 receptor × 3 (P30518) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 3 seconds before plunging. Resolution 3.96 Å

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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARRB2_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–420; UniProt 1–420 Author chain B; PDBConstruct 1–420; UniProt 1–420 Author chain C; PDBConstruct 1–420; UniProt 1–420

Vasopressin V2 receptor

OrganismNot specified

UniProt P30518

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 343–371 Chain U; UniProt 343–371 Chain V; UniProt 343–371 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-2 × 3 (P32120) Fab30 Heavy Chain × 3 Fab30 Light Chain × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 3 seconds before plunging. Resolution 3.96 Å

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.

36 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name V2R_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–29; UniProt 343–371 Author chain U; PDBConstruct 1–29; UniProt 343–371 Author chain V; PDBConstruct 1–29; UniProt 343–371

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 8i10

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8i10
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8i10
Deposition date deposition_date2023-01-12
Structure title titleStructure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Vasopressin V2 receptor, V2R (Local refine)
Keywords keywordsGPCR, Arrestin, SIGNALING PROTEIN, SIGNALING PROTEIN-IMMUNE SYSTEM complex; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.79
Radius of gyration Rg (electron density) rg_electron44.21
Forward intensity I(0) i0515773000.00
Molecular weight molecular_weight186960.0 kDa
Excluded volume excluded_volume234150 ų
Envelope volume envelope_volume344240 ų
Hydration-shell volume shell_volume65263 ų
Envelope diameter envelope_diameter142.1
Shell Rg shell_rg49.22
Envelope Rg envelope_rg42.79
Shape Rg shape_rg44.18
Total Rg total_rg44.54
Total atoms total_atoms13196
Residues n_residues1714
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 dmax142.4
Rg (real space) rg_real44.65
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real5.1580e+08
I(0) uncertainty (real space) i0_real_error9.1970e+06
Rg (reciprocal space) rg_reciprocal44.79
I(0) (reciprocal space) i0_reciprocal515900000.0000
Solution quality estimate total_estimate0.8361
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.9
Skewness Skewness skewness0.138
Kurtosis Kurtosis kurtosis-0.700
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44820000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id8i10A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily840
Domain ID domain_id8i10A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily640
Domain ID domain_id8i10B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily840
Domain ID domain_id8i10B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily640
Domain ID domain_id8i10C01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily840
Domain ID domain_id8i10C02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily640
Domain ID domain_id8i10D01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8i10E01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8i10H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8i10L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8i10M01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8i10N01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (2)

9. Files and Curves (10)