3sua

Crystal structure of the intracellular domain of Plexin-B1 in complex with Rac1

Method: X-RAY DIFFRACTION Dmax: 151.5 Å Quality: GOOD

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

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 A; UniProt 1–177 Fragment:UNP residues 1-177 Plexin-B1 × 1 (O43157) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.39 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–177 Fragment:UNP residues 1-177 Plexin-B1 × 1 (O43157) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.39 Å R-free 0.264
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–177 Fragment:UNP residues 1-177 Plexin-B1 × 1 (O43157) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.39 Å R-free 0.264
4 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–177 Chain B; UniProt 1–177 Chain C; UniProt 1–177 Fragment:UNP residues 1-177 Plexin-B1 × 3 (O43157) MG MAGNESIUM ION × 3 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.39 Å R-free 0.264

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 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–177; UniProt 1–177 Author chain B; PDBConstruct 1–177; UniProt 1–177 Author chain C; PDBConstruct 1–177; UniProt 1–177

Plexin-B1

Homo sapiens

UniProt O43157

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 D; UniProt 1511–2135 Fragment:UNP residues 1533-2135 Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.39 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1511–2135 Fragment:UNP residues 1533-2135 Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.39 Å R-free 0.264
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1511–2135 Fragment:UNP residues 1533-2135 Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.39 Å R-free 0.264
4 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1511–2135 Chain E; UniProt 1511–2135 Chain F; UniProt 1511–2135 Fragment:UNP residues 1533-2135 Ras-related C3 botulinum toxin substrate 1 × 3 (P63000) MG MAGNESIUM ION × 3 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.39 Å R-free 0.264

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.

11 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLXB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 9–633; UniProt 1511–2135 Author chain E; PDBConstruct 9–633; UniProt 1511–2135 Author chain F; PDBConstruct 9–633; UniProt 1511–2135

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 3sua

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3sua
Deposition date deposition_date2011-07-11
Structure title titleCrystal structure of the intracellular domain of Plexin-B1 in complex with Rac1
Keywords keywordsAxon guidance, signal transduction, APOPTOSIS-SIGNALING PROTEIN complex; APOPTOSIS/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.62
Radius of gyration Rg (electron density) rg_electron47.97
Forward intensity I(0) i0749534000.00
Molecular weight molecular_weight234230.0 kDa
Excluded volume excluded_volume296270 ų
Envelope volume envelope_volume429680 ų
Hydration-shell volume shell_volume73529 ų
Envelope diameter envelope_diameter152.7
Shell Rg shell_rg53.69
Envelope Rg envelope_rg46.43
Shape Rg shape_rg47.97
Total Rg total_rg48.21
Total atoms total_atoms16493
Residues n_residues2048
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 dmax151.5
Rg (real space) rg_real48.28
Rg uncertainty (real space) rg_real_error1.42
I(0) (real space) i0_real7.4950e+08
I(0) uncertainty (real space) i0_real_error1.3480e+07
Rg (reciprocal space) rg_reciprocal48.62
I(0) (reciprocal space) i0_reciprocal749900000.0000
Solution quality estimate total_estimate0.8786
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.0
Skewness Skewness skewness0.002
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44360000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.773

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)