1tx4

RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX

Method: X-RAY DIFFRACTION Dmax: 78.2 Å Quality: GOOD

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

P50-RHOGAP

Homo sapiens

UniProt Q07960

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 234–431 Not recorded TRANSFORMING PROTEIN RHOA × 1 (P61586) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;PROTEIN WAS CRYSTALLIZED FROM 18% PEG 2000 MME 100MM MES PH6.0 10MM MGCL2, 3MM DTT, 3MM NAN3, 114MM AMMONIUM SULFATE 400UM PROTEIN COMPLEX WITH 1MM ALCL3 AND 10MM NAF. Resolution 1.65 Å R-free 0.215

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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHG01_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–198; UniProt 234–431

TRANSFORMING PROTEIN RHOA

Homo sapiens

UniProt P61586

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 3–179 Not recorded P50-RHOGAP × 1 (Q07960) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;PROTEIN WAS CRYSTALLIZED FROM 18% PEG 2000 MME 100MM MES PH6.0 10MM MGCL2, 3MM DTT, 3MM NAN3, 114MM AMMONIUM SULFATE 400UM PROTEIN COMPLEX WITH 1MM ALCL3 AND 10MM NAF. Resolution 1.65 Å R-free 0.215

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.

129 other PDB entries and 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHOA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–177; UniProt 3–179

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 1tx4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1tx4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1tx4
Deposition date deposition_date1997-07-29
Structure title titleRHO/RHOGAP/GDP(DOT)ALF4 COMPLEX
Keywords keywordsCOMPLEX (GTPASE ACTIVATION-PROTO-ONCOGENE), GTPASE, TRANSITION STATE, GAP, COMPLEX(GTPASE ACTIVATN-PROTO-ONCOGENE) COMPLEX; COMPLEX(GTPASE ACTIVATN/PROTO-ONCOGENE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.51
Radius of gyration Rg (electron density) rg_electron21.50
Forward intensity I(0) i029980000.00
Molecular weight molecular_weight42520.0 kDa
Excluded volume excluded_volume53397 ų
Envelope volume envelope_volume62309 ų
Hydration-shell volume shell_volume24027 ų
Envelope diameter envelope_diameter76.5
Shell Rg shell_rg28.51
Envelope Rg envelope_rg21.83
Shape Rg shape_rg21.51
Total Rg total_rg22.33
Total atoms total_atoms2991
Residues n_residues370
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 dmax78.2
Rg (real space) rg_real22.47
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real2.9980e+07
I(0) uncertainty (real space) i0_real_error4.3360e+05
Rg (reciprocal space) rg_reciprocal22.48
I(0) (reciprocal space) i0_reciprocal29980000.0000
Solution quality estimate total_estimate0.8660
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.312
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7875000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1tx4a_
Class classa — All alpha proteins
Fold Fold folda.116 — GTPase activation domain, GAP
Superfamily Superfamily superfamilya.116.1 — GTPase activation domain, GAP
Family Family familya.116.1.1 — BCR-homology GTPase activation domain (BH-domain)
Domain ID domain_idd1tx4b_
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

CATH v4.4 (2 domains)

Domain ID domain_id1tx4A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology555 — Phosphatidylinositol 3-kinase; Chain A
Homologous superfamily homologous superfamily10 — Rho GTPase activation protein
Domain ID domain_id1tx4B00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)