7vf3

Plexin B1 extracellular fragment in complex with lasso-grafted PB1m7 peptide

Method: X-RAY DIFFRACTION Dmax: 124.1 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–535 Not recorded Uteroglobin,PB1m7 peptide,Uteroglobin × 1 (P11684) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;0.1M sodium acetate buffer, 20% PEG 400, 0.2M Calcium acetate Resolution 2.29 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 19–535 Not recorded Uteroglobin,PB1m7 peptide,Uteroglobin × 1 (P11684) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PGE TRIETHYLENE GLYCOL × 1 PG4 TETRAETHYLENE GLYCOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;0.1M sodium acetate buffer, 20% PEG 400, 0.2M Calcium acetate Resolution 2.29 Å R-free 0.226

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 23 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 1–517; UniProt 19–535 Author chain C; PDBConstruct 1–517; UniProt 19–535

Uteroglobin,PB1m7 peptide,Uteroglobin

Homo sapiens

UniProt P11684

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 21–89 Chain B; UniProt 25–91 Not recorded Plexin-B1 × 1 (O43157) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;0.1M sodium acetate buffer, 20% PEG 400, 0.2M Calcium acetate Resolution 2.29 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 21–89 Chain D; UniProt 25–91 Not recorded Plexin-B1 × 1 (O43157) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PGE TRIETHYLENE GLYCOL × 1 PG4 TETRAETHYLENE GLYCOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;0.1M sodium acetate buffer, 20% PEG 400, 0.2M Calcium acetate Resolution 2.29 Å R-free 0.226

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UTER_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–69; UniProt 21–89 Author chain B; PDBConstruct 89–155; UniProt 25–91 Author chain D; PDBConstruct 1–69; UniProt 21–89 Author chain D; PDBConstruct 89–155; UniProt 25–91

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 7vf3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7vf3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7vf3
Deposition date deposition_date2021-09-10
Structure title titlePlexin B1 extracellular fragment in complex with lasso-grafted PB1m7 peptide
Keywords keywordsPlexin, Complex, 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_guinier36.60
Radius of gyration Rg (electron density) rg_electron36.16
Forward intensity I(0) i0200668000.00
Molecular weight molecular_weight111650.0 kDa
Excluded volume excluded_volume138470 ų
Envelope volume envelope_volume179440 ų
Hydration-shell volume shell_volume42468 ų
Envelope diameter envelope_diameter124.3
Shell Rg shell_rg41.10
Envelope Rg envelope_rg35.94
Shape Rg shape_rg36.13
Total Rg total_rg36.58
Total atoms total_atoms7851
Residues n_residues1018
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 dmax124.1
Rg (real space) rg_real36.75
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real2.0070e+08
I(0) uncertainty (real space) i0_real_error3.7770e+06
Rg (reciprocal space) rg_reciprocal36.66
I(0) (reciprocal space) i0_reciprocal200600000.0000
Solution quality estimate total_estimate0.8039
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.5
Skewness Skewness skewness0.402
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21110000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.870; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)