6oya

Structure of the Rhodopsin-Transducin-Nanobody Complex

Method: ELECTRON MICROSCOPY Dmax: 120.4 Å Quality: GOOD

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

Gt-alpha/Gi1-alpha chimera

Bos taurus

UniProt P04695

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–201 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) Guanine nucleotide-binding protein G(T) subunit gamma-T1 × 1 (P02698) Camelid antibody VHH fragment × 1 Rhodopsin × 1 (P02699) RET RETINAL × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 1 second before plunging; avoid light as much as possible. Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name GNAT1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–210; UniProt 1–201

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

OrganismNot specified

UniProt P62871

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–340 Not recorded Gt-alpha/Gi1-alpha chimera × 1 (P04695) Guanine nucleotide-binding protein G(T) subunit gamma-T1 × 1 (P02698) Camelid antibody VHH fragment × 1 Rhodopsin × 1 (P02699) RET RETINAL × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 1 second before plunging; avoid light as much as possible. Resolution 3.30 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.

72 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–340; UniProt 1–340

Guanine nucleotide-binding protein G(T) subunit gamma-T1

OrganismNot specified

UniProt P02698

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 2–74 Not recorded Gt-alpha/Gi1-alpha chimera × 1 (P04695) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) Camelid antibody VHH fragment × 1 Rhodopsin × 1 (P02699) RET RETINAL × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 1 second before plunging; avoid light as much as possible. Resolution 3.30 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.

16 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG1_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 9–81; UniProt 2–74

Rhodopsin

OrganismNot specified

UniProt P02699

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 1–348 Not recorded Gt-alpha/Gi1-alpha chimera × 1 (P04695) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) Guanine nucleotide-binding protein G(T) subunit gamma-T1 × 1 (P02698) Camelid antibody VHH fragment × 1 RET RETINAL × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 1 second before plunging; avoid light as much as possible. Resolution 3.30 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.

74 other PDB entries and 95 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OPSD_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 1–348; UniProt 1–348

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 6oya

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6oya
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6oya
Deposition date deposition_date2019-05-14
Structure title titleStructure of the Rhodopsin-Transducin-Nanobody Complex
Keywords keywordsGPCR, G protein, Complex, 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_guinier35.84
Radius of gyration Rg (electron density) rg_electron35.81
Forward intensity I(0) i0212785000.00
Molecular weight molecular_weight118520.0 kDa
Excluded volume excluded_volume148650 ų
Envelope volume envelope_volume193810 ų
Hydration-shell volume shell_volume46241 ų
Envelope diameter envelope_diameter126.1
Shell Rg shell_rg41.06
Envelope Rg envelope_rg35.57
Shape Rg shape_rg35.85
Total Rg total_rg36.06
Total atoms total_atoms8321
Residues n_residues1056
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 dmax120.4
Rg (real space) rg_real35.99
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real2.1280e+08
I(0) uncertainty (real space) i0_real_error3.6210e+06
Rg (reciprocal space) rg_reciprocal35.90
I(0) (reciprocal space) i0_reciprocal212800000.0000
Solution quality estimate total_estimate0.8652
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.3
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis-0.283
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45410000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.766

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_id6oyaB00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id6oyaG00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology260 — G Protein Gi Gamma 2
Homologous superfamily homologous superfamily10 — Transducin (heterotrimeric G protein), gamma chain
Domain ID domain_id6oyaR00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily10 — Rhodopsin 7-helix transmembrane proteins

8. Citations (1)

9. Files and Curves (10)