7o1n

Crystal Structure of Human Neuropilin-1 b1 Domain mutant - Y297A

Method: X-RAY DIFFRACTION Dmax: 53.1 Å Quality: GOOD

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

Neuropilin-1

Homo sapiens

UniProt O14786

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 273–427 Mutation:Y297A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Precipitant of 20% PEG4000, 0.1M Tris (pH 8.5), 0.2M Lithium Sulfate. Protein concentration used is 10 mg/mL, mixed 1:1 with precipitant for hanging drop over reservoir of 1 mL. Resolution 1.56 Å R-free 0.209

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.

24 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NRP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–155; UniProt 273–427

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 7o1n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7o1n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7o1n
Deposition date deposition_date2021-03-29
Structure title titleCrystal Structure of Human Neuropilin-1 b1 Domain mutant - Y297A
Keywords keywordsExtracellular, Agonist domain, VEGF-A binder., PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.87
Radius of gyration Rg (electron density) rg_electron14.82
Forward intensity I(0) i05724660.00
Molecular weight molecular_weight17480.0 kDa
Excluded volume excluded_volume21945 ų
Envelope volume envelope_volume24027 ų
Hydration-shell volume shell_volume13668 ų
Envelope diameter envelope_diameter52.3
Shell Rg shell_rg20.75
Envelope Rg envelope_rg15.25
Shape Rg shape_rg14.77
Total Rg total_rg16.06
Total atoms total_atoms1232
Residues n_residues155
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 dmax53.1
Rg (real space) rg_real15.78
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real5.7250e+06
I(0) uncertainty (real space) i0_real_error6.5110e+04
Rg (reciprocal space) rg_reciprocal15.79
I(0) (reciprocal space) i0_reciprocal5725000.0000
Solution quality estimate total_estimate0.7951
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.9
Skewness Skewness skewness0.195
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1254000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.777; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)