1b9x

STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN

Method: X-RAY DIFFRACTION Dmax: 88.4 Å Quality: GOOD

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

PROTEIN (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 A; UniProt 1–340 Fragment:LYS-C RESISTANT FRAGMENT, THE BETA SUBUNIT PROTEIN (TRANSDUCIN) × 1 (P02698) PROTEIN (PHOSDUCIN) × 1 (P20942) GD GADOLINIUM ATOM × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.261

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 A; PDBConstruct 1–340; UniProt 1–340

PROTEIN (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 B; UniProt 1–67 Fragment:LYS-C RESISTANT FRAGMENT, THE GAMMA SUBUNIT CLEAVED AFTER RESIDUE 68 PROTEIN (TRANSDUCIN) × 1 (P62871) PROTEIN (PHOSDUCIN) × 1 (P20942) GD GADOLINIUM ATOM × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.261

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 B; PDBConstruct 1–68; UniProt 1–67

PROTEIN (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 C; UniProt 1–246 Mutation:S73E PROTEIN (TRANSDUCIN) × 1 (P62871) PROTEIN (TRANSDUCIN) × 1 (P02698) GD GADOLINIUM ATOM × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.00 Å R-free 0.261

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 C; PDBConstruct 1–246; UniProt 1–246

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 1b9x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b9x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b9x
Deposition date deposition_date1999-02-16
Structure title titleSTRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN
Keywords keywords;PHOSDUCIN, TRANSDUCIN, BETA-GAMMA, SIGNAL TRANSDUCTION, REGULATION, PHOSPHORYLATION, G PROTEINS, THIOREDOXIN, VISION, MEKA, COMPLEX (TRANSDUCER- TRANSDUCTION), SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.29
Radius of gyration Rg (electron density) rg_electron25.43
Forward intensity I(0) i077886600.00
Molecular weight molecular_weight65383.0 kDa
Excluded volume excluded_volume79970 ų
Envelope volume envelope_volume97876 ų
Hydration-shell volume shell_volume31870 ų
Envelope diameter envelope_diameter95.8
Shell Rg shell_rg33.08
Envelope Rg envelope_rg25.79
Shape Rg shape_rg25.40
Total Rg total_rg26.25
Total atoms total_atoms4520
Residues n_residues577
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 dmax88.4
Rg (real space) rg_real26.25
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real7.7890e+07
I(0) uncertainty (real space) i0_real_error1.1800e+06
Rg (reciprocal space) rg_reciprocal26.26
I(0) (reciprocal space) i0_reciprocal77890000.0000
Solution quality estimate total_estimate0.7996
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.222
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15200000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

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_idd1b9xa_
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_idd1b9xb_
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_idd1b9xc_
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_id1b9xA00
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_id1b9xB00
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_id1b9xC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1b9xC02
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)