6bca

A Complex between PH Domain of LbcRhoGEF (AKAP-Lbc) and Activated RhoA Bound to a GTP Analog

Method: X-RAY DIFFRACTION Dmax: 101.2 Å Quality: GOOD

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

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 F; UniProt 1–181 Not recorded A-kinase anchor protein 13 × 1 (Q12802) MG MAGNESIUM ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;24-26% PEG 3350, 100mM Bis-Tris, 200mM ammonium sulfate Resolution 2.00 Å R-free 0.234
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–181 Not recorded A-kinase anchor protein 13 × 1 (Q12802) MG MAGNESIUM ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;24-26% PEG 3350, 100mM Bis-Tris, 200mM ammonium sulfate Resolution 2.00 Å R-free 0.234

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 1
Chains and sequence ranges Author chain C; PDBConstruct 5–185; UniProt 1–181 Author chain F; PDBConstruct 5–185; UniProt 1–181

A-kinase anchor protein 13

Homo sapiens

UniProt Q12802

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 2173–2313 Not recorded Transforming protein RhoA × 1 (P61586) MG MAGNESIUM ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;24-26% PEG 3350, 100mM Bis-Tris, 200mM ammonium sulfate Resolution 2.00 Å R-free 0.234
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2173–2313 Not recorded Transforming protein RhoA × 1 (P61586) MG MAGNESIUM ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;24-26% PEG 3350, 100mM Bis-Tris, 200mM ammonium sulfate Resolution 2.00 Å R-free 0.234

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AKP13_HUMAN
Isoform Q12802-4
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 5–145; UniProt 2173–2313 Author chain B; PDBConstruct 5–145; UniProt 2173–2313

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 6bca

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6bca
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6bca
Deposition date deposition_date2017-10-20
Structure title titleA Complex between PH Domain of LbcRhoGEF (AKAP-Lbc) and Activated RhoA Bound to a GTP Analog
Keywords keywordsRho GTPase Guanine Nucleotide Exchange Factors RhoGEF Pleckstrin Homology PH domain, 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_guinier32.62
Radius of gyration Rg (electron density) rg_electron31.72
Forward intensity I(0) i087116800.00
Molecular weight molecular_weight73693.0 kDa
Excluded volume excluded_volume92260 ų
Envelope volume envelope_volume123630 ų
Hydration-shell volume shell_volume32299 ų
Envelope diameter envelope_diameter104.9
Shell Rg shell_rg38.91
Envelope Rg envelope_rg31.22
Shape Rg shape_rg31.72
Total Rg total_rg32.33
Total atoms total_atoms10354
Residues n_residues636
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 dmax101.2
Rg (real space) rg_real32.54
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real8.7120e+07
I(0) uncertainty (real space) i0_real_error1.5590e+06
Rg (reciprocal space) rg_reciprocal32.58
I(0) (reciprocal space) i0_reciprocal87120000.0000
Solution quality estimate total_estimate0.8925
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary49.5
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.788
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36440000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6bcac_
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_idd6bcaf_
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 (4 domains)

Domain ID domain_id6bcaA00
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_id6bcaB00
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_id6bcaC00
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_id6bcaF00
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)