2jph

NMR solution structure of the Rho GTPase binding domain of human plexin-b1

Method: SOLUTION NMR Dmax: 55.5 Å Quality: REASONABLE

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1743–1862 Fragment:Sequence database residues 1743-1862 Mutation:W1830F No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 0.1;Pressure ambient NMR sample composition:1.75 mM [U-100% 13C; U-100% 15N] protein, 90%H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:1.25 mM [U-100% 13C; U-100% 15N; 80% 2H] protein, 90% H2O/10% D2O | 90% H2O/10% 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 1
Chains and sequence ranges Author chain A; PDBConstruct 4–123; UniProt 1743–1862

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 2jph

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jph
Deposition date deposition_date2007-05-11
Structure title titleNMR solution structure of the Rho GTPase binding domain of human plexin-b1
Keywords keywordsprotein, ubiquitin fold, SIGNALING PROTEIN, PROTEIN BINDING; SIGNALING PROTEIN, PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.77
Radius of gyration Rg (electron density) rg_electron14.56
Forward intensity I(0) i0998212000.00
Molecular weight molecular_weight268810.0 kDa
Excluded volume excluded_volume337760 ų
Envelope volume envelope_volume42341 ų
Hydration-shell volume shell_volume19154 ų
Envelope diameter envelope_diameter65.7
Shell Rg shell_rg24.90
Envelope Rg envelope_rg18.98
Shape Rg shape_rg14.55
Total Rg total_rg14.83
Total atoms total_atoms38280
Residues n_residues2440
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 dmax55.5
Rg (real space) rg_real14.73
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real9.9820e+08
I(0) uncertainty (real space) i0_real_error1.3930e+07
Rg (reciprocal space) rg_reciprocal14.74
I(0) (reciprocal space) i0_reciprocal998200000.0000
Solution quality estimate total_estimate0.7267
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis0.038
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha428000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.508; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2jpha1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.10 — Rho GTPase binding domain
Domain ID domain_idd2jpha2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2jphA00
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

8. Citations (7)

9. Files and Curves (10)