2trc

PHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX

Method: X-RAY DIFFRACTION Dmax: 91.8 Å Quality: GOOD

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

TRANSDUCIN

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–340 Fragment:LYS-C RESISTANT FRAGMENT, THE GAMMA SUBUNIT CLEAVED AFTER RESIDUE 68 TRANSDUCIN × 1 (P02698) PHOSDUCIN × 1 (P20942) GD GADOLINIUM ATOM × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;THE PROTEIN COMPLEX (10 MG/ML SOLUTION) WAS CRYSTALLIZED FROM 50 MM SODIUM CITRATE (PH 5.0), 150 MM MAGNESIUM ACETATE, 9.5% PEG 8000, BY HANGING DROP METHOD AT 4 DEGREES C., vapor diffusion - hanging drop, temperature 277K Resolution 2.40 Å R-free 0.277

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 1
Chains and sequence ranges Author chain B; PDBConstruct 1–340; UniProt 1–340

TRANSDUCIN

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–67 Fragment:LYS-C RESISTANT FRAGMENT, THE GAMMA SUBUNIT CLEAVED AFTER RESIDUE 68 TRANSDUCIN × 1 (P62871) PHOSDUCIN × 1 (P20942) GD GADOLINIUM ATOM × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;THE PROTEIN COMPLEX (10 MG/ML SOLUTION) WAS CRYSTALLIZED FROM 50 MM SODIUM CITRATE (PH 5.0), 150 MM MAGNESIUM ACETATE, 9.5% PEG 8000, BY HANGING DROP METHOD AT 4 DEGREES C., vapor diffusion - hanging drop, temperature 277K Resolution 2.40 Å R-free 0.277

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 2
Chains and sequence ranges Author chain G; PDBConstruct 2–68; UniProt 1–67

PHOSDUCIN

Rattus norvegicus

UniProt P20942

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain P; UniProt 14–230 Non-standard monomer:Yes (specific site not provided by mmCIF) TRANSDUCIN × 1 (P62871) TRANSDUCIN × 1 (P02698) GD GADOLINIUM ATOM × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;THE PROTEIN COMPLEX (10 MG/ML SOLUTION) WAS CRYSTALLIZED FROM 50 MM SODIUM CITRATE (PH 5.0), 150 MM MAGNESIUM ACETATE, 9.5% PEG 8000, BY HANGING DROP METHOD AT 4 DEGREES C., vapor diffusion - hanging drop, temperature 277K Resolution 2.40 Å R-free 0.277

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHOS_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–217; UniProt 14–230

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 2trc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2trc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2trc
Deposition date deposition_date1997-01-06
Structure title titlePHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX
Keywords keywords;PHOSDUCIN, TRANSDUCIN, BETA-GAMMA, SIGNAL TRANSDUCTION, REGULATION, PHOSPHORYLATION, G PROTEINS, THIOREDOXIN, VISION, MEKA, COMPLEX (TRANSDUCER-TRANSDUCTION), COMPLEX (TRANSDUCER-TRANSDUCTION) complex ;; COMPLEX (TRANSDUCER/TRANSDUCTION)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.63
Radius of gyration Rg (electron density) rg_electron25.64
Forward intensity I(0) i089824200.00
Molecular weight molecular_weight69930.0 kDa
Excluded volume excluded_volume85272 ų
Envelope volume envelope_volume105830 ų
Hydration-shell volume shell_volume33664 ų
Envelope diameter envelope_diameter96.0
Shell Rg shell_rg33.72
Envelope Rg envelope_rg26.11
Shape Rg shape_rg25.60
Total Rg total_rg26.54
Total atoms total_atoms4833
Residues n_residues620
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 dmax91.8
Rg (real space) rg_real26.56
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real8.9820e+07
I(0) uncertainty (real space) i0_real_error1.2580e+06
Rg (reciprocal space) rg_reciprocal26.58
I(0) (reciprocal space) i0_reciprocal89830000.0000
Solution quality estimate total_estimate0.8677
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.312
Kurtosis Kurtosis kurtosis-0.312
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22190000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.772; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2trcb_
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.4 — WD40 repeat-like
Family Family familyb.69.4.1 — WD40-repeat
Domain ID domain_idd2trcg_
Class classa — All alpha proteins
Fold Fold folda.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamilya.137.3 — Transducin (heterotrimeric G protein), gamma chain
Family Family familya.137.3.1 — Transducin (heterotrimeric G protein), gamma chain
Domain ID domain_idd2trcp_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.6 — Phosducin

CATH v4.4 (4 domains)

Domain ID domain_id2trcB00
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_id2trcG00
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_id2trcP01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id2trcP02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology168 — Phosducin; domain 2
Homologous superfamily homologous superfamily10 — Phosducin, domain 2

8. Citations (2)

9. Files and Curves (10)