2x72

CRYSTAL STRUCTURE OF THE CONSTITUTIVELY ACTIVE E113Q,D2C,D282C RHODOPSIN MUTANT WITH BOUND GALPHACT PEPTIDE.

Method: X-RAY DIFFRACTION Dmax: 89.8 Å Quality: GOOD

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

RHODOPSIN

BOS TAURUS

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 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–348 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) GUANINE NUCLEOTIDE-BINDING PROTEIN G(T) SUBUNIT ALPHA-1 × 2 (P04695) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 2 BOG octyl beta-D-glucopyranoside × 2 PLM PALMITIC ACID × 4 RET RETINAL × 2 LPP 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE × 2 ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;3.0-3.4 M AMMONIUM SULFATE, 100 MM SODIUM ACETATE PH 4.5 Resolution 3.00 Å R-free 0.244

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 1
Chains and sequence ranges Author chain A; PDBConstruct 2–349; UniProt 1–348

GUANINE NUCLEOTIDE-BINDING PROTEIN G(T) SUBUNIT ALPHA-1

OrganismNot specified

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 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 340–350 Fragment:RESIDUES 340-350 Mutation:YES RHODOPSIN × 2 (P02699) ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 2 BOG octyl beta-D-glucopyranoside × 2 PLM PALMITIC ACID × 4 RET RETINAL × 2 LPP 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE × 2 ACT ACETATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;3.0-3.4 M AMMONIUM SULFATE, 100 MM SODIUM ACETATE PH 4.5 Resolution 3.00 Å R-free 0.244

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–11; UniProt 340–350

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 2x72

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2x72
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2x72
Deposition date deposition_date2010-02-22
Structure title titleCRYSTAL STRUCTURE OF THE CONSTITUTIVELY ACTIVE E113Q,D2C,D282C RHODOPSIN MUTANT WITH BOUND GALPHACT PEPTIDE.
Keywords keywords;SIGNALING PROTEIN, CHROMOPHORE, LIPOPROTEIN, GLYCOPROTEIN, TRANSMEMBRANE, RETINAL PROTEIN, G-PROTEIN COUPLED RECEPTOR, SENSORY TRANSDUCTION, PHOTORECEPTOR PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.29
Radius of gyration Rg (electron density) rg_electron23.18
Forward intensity I(0) i023034100.00
Molecular weight molecular_weight41342.0 kDa
Excluded volume excluded_volume53678 ų
Envelope volume envelope_volume64154 ų
Hydration-shell volume shell_volume23632 ų
Envelope diameter envelope_diameter93.2
Shell Rg shell_rg29.81
Envelope Rg envelope_rg24.03
Shape Rg shape_rg23.11
Total Rg total_rg24.37
Total atoms total_atoms2903
Residues n_residues337
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 dmax89.8
Rg (real space) rg_real24.46
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real2.3030e+07
I(0) uncertainty (real space) i0_real_error3.4440e+05
Rg (reciprocal space) rg_reciprocal24.42
I(0) (reciprocal space) i0_reciprocal23030000.0000
Solution quality estimate total_estimate0.8056
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.505
Kurtosis Kurtosis kurtosis-0.197
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4757000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.630; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.593; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2x72A00
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 (2)

9. Files and Curves (10)