6x1g

Crystal structure of a GEF domain from the Orientia tsutsugamushi protein OtDUB in complex with Rac1

Method: X-RAY DIFFRACTION Dmax: 112.7 Å Quality: GOOD

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

ULP_PROTEASE domain-containing protein

Orientia tsutsugamushi

UniProt B3CVM3

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 548–759 Fragment:GEF domain Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 9.5;293 K;25 mM CHES pH 9.5, 25% (w/v) PEG 8000 Resolution 1.60 Å R-free 0.218
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 548–759 Fragment:GEF domain Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 9.5;293 K;25 mM CHES pH 9.5, 25% (w/v) PEG 8000 Resolution 1.60 Å R-free 0.218

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.

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

View Construct and Data Evidence
UniProt name B3CVM3_ORITI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–213; UniProt 548–759 Author chain C; PDBConstruct 2–213; UniProt 548–759

Ras-related C3 botulinum toxin substrate 1

Homo sapiens

UniProt P63000

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 B; UniProt 1–177 Not recorded ULP_PROTEASE domain-containing protein × 1 (B3CVM3) X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 9.5;293 K;25 mM CHES pH 9.5, 25% (w/v) PEG 8000 Resolution 1.60 Å R-free 0.218
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–177 Not recorded ULP_PROTEASE domain-containing protein × 1 (B3CVM3) MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 9.5;293 K;25 mM CHES pH 9.5, 25% (w/v) PEG 8000 Resolution 1.60 Å R-free 0.218

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 101 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAC1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–177; UniProt 1–177 Author chain D; PDBConstruct 1–177; UniProt 1–177

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 6x1g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6x1g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6x1g
Deposition date deposition_date2020-05-18
Structure title titleCrystal structure of a GEF domain from the Orientia tsutsugamushi protein OtDUB in complex with Rac1
Keywords keywords;guanine nucleotide exchange factor, GEF, Rac1, GTPase, Orientia tsutsugamushi, scrub typhus, SIGNALING PROTEIN, SIGNALING PROTEIN-HYDROLASE complex ;; SIGNALING PROTEIN/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.13
Radius of gyration Rg (electron density) rg_electron33.65
Forward intensity I(0) i0120593000.00
Molecular weight molecular_weight89072.0 kDa
Excluded volume excluded_volume112150 ų
Envelope volume envelope_volume146710 ų
Hydration-shell volume shell_volume37429 ų
Envelope diameter envelope_diameter117.2
Shell Rg shell_rg39.01
Envelope Rg envelope_rg33.62
Shape Rg shape_rg33.66
Total Rg total_rg34.04
Total atoms total_atoms6267
Residues n_residues788
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 dmax112.7
Rg (real space) rg_real34.26
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.2060e+08
I(0) uncertainty (real space) i0_real_error2.1360e+06
Rg (reciprocal space) rg_reciprocal34.18
I(0) (reciprocal space) i0_reciprocal120600000.0000
Solution quality estimate total_estimate0.8771
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.3
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16700000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.950; Smooth: 0.895

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6x1gb1
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_idd6x1gb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6x1gd1
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_idd6x1gd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)