4qds

Physical basis for Nrp2 ligand binding

Method: X-RAY DIFFRACTION Dmax: 95.0 Å Quality: GOOD

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

Neuropilin-2

Homo sapiens

UniProt O60462

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 275–457 Chain B; UniProt 275–457 Fragment:Proteolytic fragment of s9Nrp2 coagulation factor domains GOL GLYCEROL × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;10% PEG 1000, 10% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.40 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.

15 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NRP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–187; UniProt 275–457 Author chain B; PDBConstruct 5–187; UniProt 275–457

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 4qds

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qds
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4qds
Deposition date deposition_date2014-05-14
Structure title titlePhysical basis for Nrp2 ligand binding
Keywords keywordscoagulation factor domain, discoidin domain, receptor, VEGF-C, secreted, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.57
Radius of gyration Rg (electron density) rg_electron26.99
Forward intensity I(0) i030062700.00
Molecular weight molecular_weight40578.0 kDa
Excluded volume excluded_volume50102 ų
Envelope volume envelope_volume61856 ų
Hydration-shell volume shell_volume21485 ų
Envelope diameter envelope_diameter99.5
Shell Rg shell_rg30.77
Envelope Rg envelope_rg26.78
Shape Rg shape_rg27.08
Total Rg total_rg27.13
Total atoms total_atoms2850
Residues n_residues361
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 dmax95.0
Rg (real space) rg_real27.98
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real3.0060e+07
I(0) uncertainty (real space) i0_real_error4.8140e+05
Rg (reciprocal space) rg_reciprocal27.86
I(0) (reciprocal space) i0_reciprocal30060000.0000
Solution quality estimate total_estimate0.7783
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.585
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8310000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.574; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.547; Smooth: 0.844

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4qdsA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id4qdsB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like

8. Citations (1)

9. Files and Curves (10)