1g4u

CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1

Method: X-RAY DIFFRACTION Dmax: 102.3 Å Quality: GOOD

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

PROTEIN TYROSINE PHOSPHATASE SPTP

Salmonella typhimurium

UniProt P74873

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 S; UniProt 161–543 Fragment:SPTP RESIDUES 161-543 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 (P63000) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;18 %PEG 400, 0.1M MES, 15mM sodium flouride, 0.1mM aluminum chloride, 2mM DTT, 2mM magnesium chloride, pH 5.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.30 Å R-free 0.258

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 SPTP_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain S; PDBConstruct 1–383; UniProt 161–543

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 R; UniProt 1–184 Fragment:RAC1 RESIDUES 1-184 Mutation:F78S PROTEIN TYROSINE PHOSPHATASE SPTP × 1 (P74873) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;18 %PEG 400, 0.1M MES, 15mM sodium flouride, 0.1mM aluminum chloride, 2mM DTT, 2mM magnesium chloride, pH 5.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.30 Å R-free 0.258

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 102 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 R; PDBConstruct 1–184; UniProt 1–184

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 1g4u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g4u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1g4u
Deposition date deposition_date2000-10-28
Structure title titleCRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1
Keywords keywordsvirulence factor, GAP, tyrosine phosphatase, 4-helix bundle, GTPase, 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_guinier30.10
Radius of gyration Rg (electron density) rg_electron29.92
Forward intensity I(0) i060341100.00
Molecular weight molecular_weight60319.0 kDa
Excluded volume excluded_volume75321 ų
Envelope volume envelope_volume95719 ų
Hydration-shell volume shell_volume28316 ų
Envelope diameter envelope_diameter108.2
Shell Rg shell_rg34.99
Envelope Rg envelope_rg29.80
Shape Rg shape_rg29.93
Total Rg total_rg30.39
Total atoms total_atoms4221
Residues n_residues540
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 dmax102.3
Rg (real space) rg_real30.33
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real6.0340e+07
I(0) uncertainty (real space) i0_real_error9.0140e+05
Rg (reciprocal space) rg_reciprocal30.24
I(0) (reciprocal space) i0_reciprocal60340000.0000
Solution quality estimate total_estimate0.8386
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.486
Kurtosis Kurtosis kurtosis-0.484
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha28850000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.733; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.750; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1g4ur_
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_idd1g4us1
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.11 — Bacterial GAP domain
Family Family familya.24.11.1 — Bacterial GAP domain
Domain ID domain_idd1g4us2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.45 — (Phosphotyrosine protein) phosphatases II
Superfamily Superfamily superfamilyc.45.1 — (Phosphotyrosine protein) phosphatases II
Family Family familyc.45.1.2 — Higher-molecular-weight phosphotyrosine protein phosphatases

CATH v4.4 (3 domains)

Domain ID domain_id1g4uR00
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_id1g4uS01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily260 — Virulence factor YopE uncharacterised domain
Domain ID domain_id1g4uS02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology190 — Protein-Tyrosine Phosphatase; Chain A
Homologous superfamily homologous superfamily10 — Protein tyrosine phosphatase superfamily

8. Citations (1)

9. Files and Curves (10)