1xcg

Crystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF

Method: X-RAY DIFFRACTION Dmax: 148.2 Å Quality: GOOD

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

Rho guanine nucleotide exchange factor 11

Homo sapiens

UniProt O15085

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 714–1081 Fragment:DH/PH domain Transforming protein RhoA × 1 (P61586) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;298 K;PEG, Hepes, pH 7.2, VAPOR DIFFUSION, temperature 298K Resolution 2.50 Å R-free 0.281
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 714–1081 Fragment:DH/PH domain Transforming protein RhoA × 1 (P61586) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;298 K;PEG, Hepes, pH 7.2, VAPOR DIFFUSION, temperature 298K Resolution 2.50 Å R-free 0.281

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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARHGB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–368; UniProt 714–1081 Author chain E; PDBConstruct 1–368; UniProt 714–1081

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 3–180 Fragment:RhoA Mutation:F25N Rho guanine nucleotide exchange factor 11 × 1 (O15085) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;298 K;PEG, Hepes, pH 7.2, VAPOR DIFFUSION, temperature 298K Resolution 2.50 Å R-free 0.281
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 3–180 Fragment:RhoA Mutation:F25N Rho guanine nucleotide exchange factor 11 × 1 (O15085) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;298 K;PEG, Hepes, pH 7.2, VAPOR DIFFUSION, temperature 298K Resolution 2.50 Å R-free 0.281

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 164 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 1–178; UniProt 3–180 Author chain F; PDBConstruct 1–178; UniProt 3–180

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 1xcg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xcg
Deposition date deposition_date2004-09-01
Structure title titleCrystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF
Keywords keywordsX-ray crystallography; regulation of RhoA GTPase; protein complex, SIGNALING PROTEIN ACTIVATOR-SIGNALING PROTEIN COMPLEX; SIGNALING PROTEIN ACTIVATOR/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.71
Radius of gyration Rg (electron density) rg_electron43.85
Forward intensity I(0) i0226657000.00
Molecular weight molecular_weight123410.0 kDa
Excluded volume excluded_volume155030 ų
Envelope volume envelope_volume220410 ų
Hydration-shell volume shell_volume44967 ų
Envelope diameter envelope_diameter153.2
Shell Rg shell_rg44.50
Envelope Rg envelope_rg42.66
Shape Rg shape_rg43.86
Total Rg total_rg43.86
Total atoms total_atoms8659
Residues n_residues1069
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 dmax148.2
Rg (real space) rg_real44.09
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real2.2670e+08
I(0) uncertainty (real space) i0_real_error3.7800e+06
Rg (reciprocal space) rg_reciprocal43.71
I(0) (reciprocal space) i0_reciprocal226600000.0000
Solution quality estimate total_estimate0.8092
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.432
Kurtosis Kurtosis kurtosis-0.730
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23320000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.665; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.674; Smooth: 0.845

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1xcga1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd1xcga2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)
Domain ID domain_idd1xcgb_
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_idd1xcge1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd1xcge2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)
Domain ID domain_idd1xcgf_
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 (6 domains)

Domain ID domain_id1xcgA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id1xcgA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id1xcgB00
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_id1xcgE01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id1xcgE02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id1xcgF00
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)