3ryt

The Plexin A1 intracellular region in complex with Rac1

Method: X-RAY DIFFRACTION Dmax: 129.5 Å Quality: GOOD

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

Plexin-A1

Mus musculus

UniProt P70206

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 1269–1894 Fragment:intracellular region (UNP residues 1269-1894) Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;15% PEG1500, 100 mM SPG buffer, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.58 Å R-free 0.340
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1269–1894 Fragment:intracellular region (UNP residues 1269-1894) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;15% PEG1500, 100 mM SPG buffer, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.58 Å R-free 0.340

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLXA1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–626; UniProt 1269–1894 Author chain B; PDBConstruct 1–626; UniProt 1269–1894

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 C; UniProt 1–177 Fragment:UNP residues 1-177 Mutation:Q61L Plexin-A1 × 1 (P70206) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;15% PEG1500, 100 mM SPG buffer, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.58 Å R-free 0.340

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 C; PDBConstruct 4–180; 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 3ryt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ryt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ryt
Deposition date deposition_date2011-05-11
Structure title titleThe Plexin A1 intracellular region in complex with Rac1
Keywords keywordsplexin, RasGAP, GTPase activating protein, Rac, 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_guinier37.85
Radius of gyration Rg (electron density) rg_electron37.31
Forward intensity I(0) i0258883000.00
Molecular weight molecular_weight129200.0 kDa
Excluded volume excluded_volume161220 ų
Envelope volume envelope_volume229950 ų
Hydration-shell volume shell_volume52545 ų
Envelope diameter envelope_diameter134.2
Shell Rg shell_rg42.27
Envelope Rg envelope_rg37.28
Shape Rg shape_rg37.30
Total Rg total_rg37.67
Total atoms total_atoms9112
Residues n_residues1237
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 dmax129.5
Rg (real space) rg_real37.94
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real2.5890e+08
I(0) uncertainty (real space) i0_real_error4.2680e+06
Rg (reciprocal space) rg_reciprocal37.88
I(0) (reciprocal space) i0_reciprocal258900000.0000
Solution quality estimate total_estimate0.8593
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.2
Skewness Skewness skewness0.454
Kurtosis Kurtosis kurtosis-0.093
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha53760000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.798

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id3rytA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology506 — GTPase Activation - p120GAP; domain 1
Homologous superfamily homologous superfamily10 — GTPase Activation - p120gap; domain 1
Domain ID domain_id3rytA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id3rytB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology506 — GTPase Activation - p120GAP; domain 1
Homologous superfamily homologous superfamily10 — GTPase Activation - p120gap; domain 1
Domain ID domain_id3rytB02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id3rytC00
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)