2os6

Solution structure of LARG PDZ domain in complex with C-terminal octa-peptide of Plexin B1

Method: SOLUTION NMR Dmax: 54.0 Å Quality: REASONABLE

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

Rho guanine nucleotide exchange factor 12

Homo sapiens

UniProt Q9NZN5

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 67–151 Fragment:PDZ domain C-terminal peptide of Plexin-B1 × 1 (O43157) SOLUTION NMR NMR measurement conditions:pH 6;293 K;Ionic strength (raw mmCIF value) 50 mM phosphate buffer, 50mM NaCl;Pressure 1 NMR sample composition:0.8mM 15N, 13C-labeled LARG PDZ domain, 5mM EDTA, 1mM DTT, 7.6mM synthetic peptide, 50mM phosphate buffer, 90% H2O, 10% D2O | 50mM phosphate buffer, 90% H2O, 10% D2O NMR sample composition:0.8mM 15N, 13C-labeled LARG PDZ domain, 5mM EDTA, 1mM DTT, 7.6mM synthetic peptide, 50mM phosphate buffer, 99.9% D2O | 50mM phosphate buffer, 99.9% D2O Resolution not provided

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARHGC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–89; UniProt 67–151

C-terminal peptide of Plexin-B1

OrganismNot specified

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 B; UniProt 2128–2135 Not recorded Rho guanine nucleotide exchange factor 12 × 1 (Q9NZN5) SOLUTION NMR NMR measurement conditions:pH 6;293 K;Ionic strength (raw mmCIF value) 50 mM phosphate buffer, 50mM NaCl;Pressure 1 NMR sample composition:0.8mM 15N, 13C-labeled LARG PDZ domain, 5mM EDTA, 1mM DTT, 7.6mM synthetic peptide, 50mM phosphate buffer, 90% H2O, 10% D2O | 50mM phosphate buffer, 90% H2O, 10% D2O NMR sample composition:0.8mM 15N, 13C-labeled LARG PDZ domain, 5mM EDTA, 1mM DTT, 7.6mM synthetic peptide, 50mM phosphate buffer, 99.9% D2O | 50mM phosphate buffer, 99.9% D2O Resolution not provided

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 24 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 B; PDBConstruct 1–8; UniProt 2128–2135

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 2os6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2os6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2os6
Deposition date deposition_date2007-02-05
Structure title titleSolution structure of LARG PDZ domain in complex with C-terminal octa-peptide of Plexin B1
Keywords keywordsnerve system development, cytoskeleton rearrangement, cell adhesion; CELL ADHESION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.05
Radius of gyration Rg (electron density) rg_electron13.48
Forward intensity I(0) i0619910000.00
Molecular weight molecular_weight205520.0 kDa
Excluded volume excluded_volume255990 ų
Envelope volume envelope_volume30665 ų
Hydration-shell volume shell_volume15470 ų
Envelope diameter envelope_diameter55.2
Shell Rg shell_rg22.85
Envelope Rg envelope_rg17.66
Shape Rg shape_rg13.46
Total Rg total_rg13.76
Total atoms total_atoms29220
Residues n_residues1940
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 dmax54.0
Rg (real space) rg_real14.04
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real6.1990e+08
I(0) uncertainty (real space) i0_real_error7.5920e+06
Rg (reciprocal space) rg_reciprocal14.04
I(0) (reciprocal space) i0_reciprocal619900000.0000
Solution quality estimate total_estimate0.7058
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary17.1
Skewness Skewness skewness0.336
Kurtosis Kurtosis kurtosis-0.044
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha239500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.433; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2os6A00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology42 — Pdz3 Domain
Homologous superfamily homologous superfamily10 — PDZ domain

8. Citations (1)

9. Files and Curves (10)