1agr

COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4

Method: X-RAY DIFFRACTION Dmax: 122.7 Å Quality: GOOD

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

GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)

Rattus norvegicus

UniProt P10824

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–353 Fragment:ALPHA-1 RGS4 × 1 (P49799) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;THE COMPLEX WAS CRYSTALLIZED IN HANGING DROPS USING PEG 10000 AS THE PRECIPITANT AND SODIUM CITRATE PH 5.3 AS THE BUFFER., vapor diffusion - hanging drop Resolution 2.80 Å R-free 0.291
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–353 Fragment:ALPHA-1 RGS4 × 1 (P49799) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;THE COMPLEX WAS CRYSTALLIZED IN HANGING DROPS USING PEG 10000 AS THE PRECIPITANT AND SODIUM CITRATE PH 5.3 AS THE BUFFER., vapor diffusion - hanging drop Resolution 2.80 Å R-free 0.291

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.

43 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBI1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–353; UniProt 1–353 Author chain D; PDBConstruct 1–353; UniProt 1–353

RGS4

Rattus norvegicus

UniProt P49799

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–205 Not recorded GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) × 1 (P10824) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;THE COMPLEX WAS CRYSTALLIZED IN HANGING DROPS USING PEG 10000 AS THE PRECIPITANT AND SODIUM CITRATE PH 5.3 AS THE BUFFER., vapor diffusion - hanging drop Resolution 2.80 Å R-free 0.291
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1–205 Not recorded GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) × 1 (P10824) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;THE COMPLEX WAS CRYSTALLIZED IN HANGING DROPS USING PEG 10000 AS THE PRECIPITANT AND SODIUM CITRATE PH 5.3 AS THE BUFFER., vapor diffusion - hanging drop Resolution 2.80 Å R-free 0.291

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 RGS4_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–205; UniProt 1–205 Author chain H; PDBConstruct 1–205; UniProt 1–205

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 1agr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1agr
Deposition date deposition_date1997-03-25
Structure title titleCOMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4
Keywords keywords;GI-ALPHA-1, HYDROLASE, SIGNAL TRANSDUCTION, RGS4, COMPLEX (SIGNAL TRANSDUCTION-REGULATOR), GTP-BINDING, GTPASE ACTIVATING PROTEIN, COMPLEX (SIGNAL TRANSDUCTION-REGULATOR) complex ;; COMPLEX (SIGNAL TRANSDUCTION/REGULATOR)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.91
Radius of gyration Rg (electron density) rg_electron34.75
Forward intensity I(0) i0187820000.00
Molecular weight molecular_weight109410.0 kDa
Excluded volume excluded_volume136560 ų
Envelope volume envelope_volume175630 ų
Hydration-shell volume shell_volume42478 ų
Envelope diameter envelope_diameter132.4
Shell Rg shell_rg40.52
Envelope Rg envelope_rg35.24
Shape Rg shape_rg34.72
Total Rg total_rg35.23
Total atoms total_atoms7674
Residues n_residues938
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 dmax122.7
Rg (real space) rg_real34.99
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real1.8780e+08
I(0) uncertainty (real space) i0_real_error3.0340e+06
Rg (reciprocal space) rg_reciprocal34.94
I(0) (reciprocal space) i0_reciprocal187800000.0000
Solution quality estimate total_estimate0.8673
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.4
Skewness Skewness skewness0.401
Kurtosis Kurtosis kurtosis-0.331
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26510000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.937; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1agra1
Class classa — All alpha proteins
Fold Fold folda.66 — Transducin (alpha subunit), insertion domain
Superfamily Superfamily superfamilya.66.1 — Transducin (alpha subunit), insertion domain
Family Family familya.66.1.1 — Transducin (alpha subunit), insertion domain
Domain ID domain_idd1agra2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1agrd1
Class classa — All alpha proteins
Fold Fold folda.66 — Transducin (alpha subunit), insertion domain
Superfamily Superfamily superfamilya.66.1 — Transducin (alpha subunit), insertion domain
Family Family familya.66.1.1 — Transducin (alpha subunit), insertion domain
Domain ID domain_idd1agrd2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1agre_
Class classa — All alpha proteins
Fold Fold folda.91 — Regulator of G-protein signaling, RGS
Superfamily Superfamily superfamilya.91.1 — Regulator of G-protein signaling, RGS
Family Family familya.91.1.1 — Regulator of G-protein signaling, RGS
Domain ID domain_idd1agrh_
Class classa — All alpha proteins
Fold Fold folda.91 — Regulator of G-protein signaling, RGS
Superfamily Superfamily superfamilya.91.1 — Regulator of G-protein signaling, RGS
Family Family familya.91.1.1 — Regulator of G-protein signaling, RGS

CATH v4.4 (8 domains)

Domain ID domain_id1agrA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1agrA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like
Domain ID domain_id1agrD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1agrD02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like
Domain ID domain_id1agrE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology196 — Regulator of G-protein Signalling 4; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id1agrE02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily10 — Regulator of G-protein Signalling 4, domain 2
Domain ID domain_id1agrH01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology196 — Regulator of G-protein Signalling 4; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id1agrH02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology167 — Regulator of G-protein Signalling 4; domain 2
Homologous superfamily homologous superfamily10 — Regulator of G-protein Signalling 4, domain 2

8. Citations (1)

9. Files and Curves (10)