1shz

Crystal Structure of the p115RhoGEF rgRGS Domain in A Complex with Galpha(13):Galpha(i1) Chimera

Method: X-RAY DIFFRACTION Dmax: 111.9 Å Quality: GOOD

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

Guanine Nucleotide-Binding Protein Galpha(13):Galpha(i1) Chimera

Mus musculus

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 21–47 Chain A; UniProt 185–210 Chain A; UniProt 213–230 Chain A; UniProt 240–353 Fragment:residues 21-47, 185-210, 213-230, 240-353 of Galpha(i1) and residues 64-207, 234-235, 254-262 of Galpha(13) Rho guanine nucleotide exchange factor 1 × 1 (Q92888) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 21–47 Chain D; UniProt 185–210 Chain D; UniProt 213–230 Chain D; UniProt 240–353 Fragment:residues 21-47, 185-210, 213-230, 240-353 of Galpha(i1) and residues 64-207, 234-235, 254-262 of Galpha(13) Rho guanine nucleotide exchange factor 1 × 1 (Q92888) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297
3 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 21–47 Chain A; UniProt 185–210 Chain A; UniProt 213–230 Chain A; UniProt 240–353 Chain D; UniProt 21–47 Chain D; UniProt 185–210 Chain D; UniProt 213–230 Chain D; UniProt 240–353 Fragment:residues 21-47, 185-210, 213-230, 240-353 of Galpha(i1) and residues 64-207, 234-235, 254-262 of Galpha(13) Rho guanine nucleotide exchange factor 1 × 2 (Q92888) MG MAGNESIUM ION × 2 ALF TETRAFLUOROALUMINATE ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297

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 55 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 1–27; UniProt 21–47 Author chain A; PDBConstruct 172–197; UniProt 185–210 Author chain A; PDBConstruct 200–217; UniProt 213–230 Author chain A; PDBConstruct 227–340; UniProt 240–353 Author chain D; PDBConstruct 1–27; UniProt 21–47 Author chain D; PDBConstruct 172–197; UniProt 185–210 Author chain D; PDBConstruct 200–217; UniProt 213–230 Author chain D; PDBConstruct 227–340; UniProt 240–353

Guanine Nucleotide-Binding Protein Galpha(13):Galpha(i1) Chimera

Mus musculus

UniProt P27601

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 64–207 Chain A; UniProt 234–235 Chain A; UniProt 254–262 Fragment:residues 21-47, 185-210, 213-230, 240-353 of Galpha(i1) and residues 64-207, 234-235, 254-262 of Galpha(13) Rho guanine nucleotide exchange factor 1 × 1 (Q92888) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 64–207 Chain D; UniProt 234–235 Chain D; UniProt 254–262 Fragment:residues 21-47, 185-210, 213-230, 240-353 of Galpha(i1) and residues 64-207, 234-235, 254-262 of Galpha(13) Rho guanine nucleotide exchange factor 1 × 1 (Q92888) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297
3 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 64–207 Chain A; UniProt 234–235 Chain A; UniProt 254–262 Chain D; UniProt 64–207 Chain D; UniProt 234–235 Chain D; UniProt 254–262 Fragment:residues 21-47, 185-210, 213-230, 240-353 of Galpha(i1) and residues 64-207, 234-235, 254-262 of Galpha(13) Rho guanine nucleotide exchange factor 1 × 2 (Q92888) MG MAGNESIUM ION × 2 ALF TETRAFLUOROALUMINATE ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GB13_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 28–171; UniProt 64–207 Author chain A; PDBConstruct 198–199; UniProt 234–235 Author chain A; PDBConstruct 218–226; UniProt 254–262 Author chain D; PDBConstruct 28–171; UniProt 64–207 Author chain D; PDBConstruct 198–199; UniProt 234–235 Author chain D; PDBConstruct 218–226; UniProt 254–262

Rho guanine nucleotide exchange factor 1

Homo sapiens

UniProt Q92888

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 7–239 Fragment:N-terminal RhoGEF RGS (rgRGS) domain of p115RhoGEF (residues 7-239) Guanine Nucleotide-Binding Protein Galpha(13):Galpha(i1) Chimera × 1 (P10824,P27601) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 7–239 Fragment:N-terminal RhoGEF RGS (rgRGS) domain of p115RhoGEF (residues 7-239) Guanine Nucleotide-Binding Protein Galpha(13):Galpha(i1) Chimera × 1 (P10824,P27601) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297
3 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 7–239 Chain F; UniProt 7–239 Fragment:N-terminal RhoGEF RGS (rgRGS) domain of p115RhoGEF (residues 7-239) Guanine Nucleotide-Binding Protein Galpha(13):Galpha(i1) Chimera × 2 (P10824,P27601) MG MAGNESIUM ION × 2 ALF TETRAFLUOROALUMINATE ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;Ammonium Sulfate, Tris, Ethylene glycol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.85 Å R-free 0.297

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.

6 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARHG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–233; UniProt 7–239 Author chain F; PDBConstruct 1–233; UniProt 7–239

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 1shz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1shz
Deposition date deposition_date2004-02-26
Structure title titleCrystal Structure of the p115RhoGEF rgRGS Domain in A Complex with Galpha(13):Galpha(i1) Chimera
Keywords keywordsSIGNAL TRANSDUCTION, PROTEIN COMPLEX, 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_guinier33.88
Radius of gyration Rg (electron density) rg_electron33.59
Forward intensity I(0) i0230686000.00
Molecular weight molecular_weight121190.0 kDa
Excluded volume excluded_volume151320 ų
Envelope volume envelope_volume197800 ų
Hydration-shell volume shell_volume48590 ų
Envelope diameter envelope_diameter121.6
Shell Rg shell_rg40.68
Envelope Rg envelope_rg33.74
Shape Rg shape_rg33.61
Total Rg total_rg34.05
Total atoms total_atoms8518
Residues n_residues1037
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 dmax111.9
Rg (real space) rg_real33.83
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real2.3070e+08
I(0) uncertainty (real space) i0_real_error3.7530e+06
Rg (reciprocal space) rg_reciprocal33.86
I(0) (reciprocal space) i0_reciprocal230700000.0000
Solution quality estimate total_estimate0.8915
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.5
Skewness Skewness skewness0.301
Kurtosis Kurtosis kurtosis-0.354
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97920000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1shza1
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_idd1shza2
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_idd1shzc_
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.91.1.0 — automated matches
Domain ID domain_idd1shzd1
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_idd1shzd2
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_idd1shzf_
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.91.1.0 — automated matches

CATH v4.4 (6 domains)

Domain ID domain_id1shzA01
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_id1shzA02
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_id1shzC00
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_id1shzD01
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_id1shzD02
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_id1shzF00
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)