1hh4

Rac1-RhoGDI complex involved in NADPH oxidase activation

Method: X-RAY DIFFRACTION Dmax: 117.9 Å Quality: GOOD

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

RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1

HOMO SAPIENS

UniProt P15154

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 1–192 Not recorded RHO GDP-DISSOCIATION INHIBITOR 1 × 1 (P52565) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GER GERAN-8-YL GERAN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;HANGING DROP AT 20C WITH RESERVOIR: 30% PEG 4000, 100 MM NA CITRATE PH=5.6, 5 MM MGCL2, 200 MM AMMONIUM ACETATE, pH 5.60 Resolution 2.70 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–192 Not recorded RHO GDP-DISSOCIATION INHIBITOR 1 × 1 (P52565) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GER GERAN-8-YL GERAN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;HANGING DROP AT 20C WITH RESERVOIR: 30% PEG 4000, 100 MM NA CITRATE PH=5.6, 5 MM MGCL2, 200 MM AMMONIUM ACETATE, pH 5.60 Resolution 2.70 Å R-free 0.280

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–192; UniProt 1–192 Author chain B; PDBConstruct 1–192; UniProt 1–192

RHO GDP-DISSOCIATION INHIBITOR 1

HOMO SAPIENS

UniProt P52565

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 D; UniProt 1–204 Not recorded RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 (P15154) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GER GERAN-8-YL GERAN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;HANGING DROP AT 20C WITH RESERVOIR: 30% PEG 4000, 100 MM NA CITRATE PH=5.6, 5 MM MGCL2, 200 MM AMMONIUM ACETATE, pH 5.60 Resolution 2.70 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–204 Not recorded RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 (P15154) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GER GERAN-8-YL GERAN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;293 K;HANGING DROP AT 20C WITH RESERVOIR: 30% PEG 4000, 100 MM NA CITRATE PH=5.6, 5 MM MGCL2, 200 MM AMMONIUM ACETATE, pH 5.60 Resolution 2.70 Å R-free 0.280

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.

20 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GDIR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–204; UniProt 1–204 Author chain E; PDBConstruct 1–204; UniProt 1–204

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 1hh4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1hh4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1hh4
Deposition date deposition_date2000-12-20
Structure title titleRac1-RhoGDI complex involved in NADPH oxidase activation
Keywords keywords;SIGNALING PROTEIN/INHIBITOR, SINGAL PROTEIN INHIBITOR COMPLEX, SMALL G PROTEIN, GTPASE ACTIVATION, GTP-BINDING, PRENYLATION, LIPOPROTEIN, SIGNALING PROTEIN-INHIBITOR complex ;; SIGNALING PROTEIN/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.01
Radius of gyration Rg (electron density) rg_electron35.62
Forward intensity I(0) i0105710000.00
Molecular weight molecular_weight83588.0 kDa
Excluded volume excluded_volume105140 ų
Envelope volume envelope_volume148490 ų
Hydration-shell volume shell_volume35134 ų
Envelope diameter envelope_diameter120.0
Shell Rg shell_rg41.92
Envelope Rg envelope_rg34.48
Shape Rg shape_rg35.59
Total Rg total_rg36.17
Total atoms total_atoms5878
Residues n_residues744
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 dmax117.9
Rg (real space) rg_real36.04
Rg uncertainty (real space) rg_real_error1.16
I(0) (real space) i0_real1.0570e+08
I(0) uncertainty (real space) i0_real_error1.7320e+06
Rg (reciprocal space) rg_reciprocal36.03
I(0) (reciprocal space) i0_reciprocal105700000.0000
Solution quality estimate total_estimate0.8826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.9
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.709
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20480000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.887

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1hh4a1
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_idd1hh4a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1hh4b1
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_idd1hh4b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1hh4d_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.8 — RhoGDI-like
Domain ID domain_idd1hh4e_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.8 — RhoGDI-like

CATH v4.4 (4 domains)

Domain ID domain_id1hh4A00
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_id1hh4B00
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_id1hh4D00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily30 — Coagulation Factor XIII, subunit A, domain 1
Domain ID domain_id1hh4E00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily30 — Coagulation Factor XIII, subunit A, domain 1

8. Citations (1)

9. Files and Curves (10)