5dn2

Human NRP2 b1 domain in complex with the peptide corresponding to the C-terminus of VEGF-A

Method: X-RAY DIFFRACTION Dmax: 94.8 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 275–429 Fragment:Neuropilin-2 domain B1 F5/8 type C 1, UNP residues 275-429 Vascular endothelial growth factor A × 1 (P15692) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;289 K;10% PEG20000, 0.1M Bicine, 2% v/v dioxane Resolution 1.95 Å R-free 0.234
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 275–429 Fragment:Neuropilin-2 domain B1 F5/8 type C 1, UNP residues 275-429 DIO 1,4-DIETHYLENE DIOXIDE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;289 K;10% PEG20000, 0.1M Bicine, 2% v/v dioxane Resolution 1.95 Å R-free 0.234
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 275–429 Fragment:Neuropilin-2 domain B1 F5/8 type C 1, UNP residues 275-429 Vascular endothelial growth factor A × 1 (P15692) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;289 K;10% PEG20000, 0.1M Bicine, 2% v/v dioxane Resolution 1.95 Å R-free 0.234
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 275–429 Fragment:Neuropilin-2 domain B1 F5/8 type C 1, UNP residues 275-429 Vascular endothelial growth factor A × 1 (P15692) DIO 1,4-DIETHYLENE DIOXIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;289 K;10% PEG20000, 0.1M Bicine, 2% v/v dioxane Resolution 1.95 Å R-free 0.234

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 28 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 2–156; UniProt 275–429 Author chain B; PDBConstruct 2–156; UniProt 275–429 Author chain C; PDBConstruct 2–156; UniProt 275–429 Author chain D; PDBConstruct 2–156; UniProt 275–429

Vascular endothelial growth factor A

Homo sapiens

UniProt P15692

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 G; UniProt 205–232 Fragment:VEGF-A165-HBD, UNP residues 205-232 Neuropilin-2 × 1 (O60462) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;289 K;10% PEG20000, 0.1M Bicine, 2% v/v dioxane Resolution 1.95 Å R-free 0.234
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 205–232 Fragment:VEGF-A165-HBD, UNP residues 205-232 Neuropilin-2 × 1 (O60462) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;289 K;10% PEG20000, 0.1M Bicine, 2% v/v dioxane Resolution 1.95 Å R-free 0.234
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 205–232 Fragment:VEGF-A165-HBD, UNP residues 205-232 Neuropilin-2 × 1 (O60462) DIO 1,4-DIETHYLENE DIOXIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;289 K;10% PEG20000, 0.1M Bicine, 2% v/v dioxane Resolution 1.95 Å R-free 0.234

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.

50 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VEGFA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–28; UniProt 205–232 Author chain F; PDBConstruct 1–28; UniProt 205–232 Author chain G; PDBConstruct 1–28; UniProt 205–232

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 5dn2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5dn2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5dn2
Deposition date deposition_date2015-09-09
Structure title titleHuman NRP2 b1 domain in complex with the peptide corresponding to the C-terminus of VEGF-A
Keywords keywordsSIGNALING PROTEIN, Neuropilin-2, VEGFA, Angiogenesis, heparin, receptor; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.11
Radius of gyration Rg (electron density) rg_electron29.65
Forward intensity I(0) i093852900.00
Molecular weight molecular_weight73588.0 kDa
Excluded volume excluded_volume90997 ų
Envelope volume envelope_volume117430 ų
Hydration-shell volume shell_volume33551 ų
Envelope diameter envelope_diameter102.5
Shell Rg shell_rg36.16
Envelope Rg envelope_rg29.46
Shape Rg shape_rg29.58
Total Rg total_rg30.47
Total atoms total_atoms5178
Residues n_residues640
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 dmax94.8
Rg (real space) rg_real29.99
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real9.3850e+07
I(0) uncertainty (real space) i0_real_error1.4230e+06
Rg (reciprocal space) rg_reciprocal30.04
I(0) (reciprocal space) i0_reciprocal93860000.0000
Solution quality estimate total_estimate0.9080
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.9
Skewness Skewness skewness0.118
Kurtosis Kurtosis kurtosis-0.603
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23040000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd5dn2a1
Class classb — All beta proteins
Fold Fold foldb.18 — Galactose-binding domain-like
Superfamily Superfamily superfamilyb.18.1 — Galactose-binding domain-like
Family Family familyb.18.1.0 — automated matches
Domain ID domain_idd5dn2a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5dn2b1
Class classb — All beta proteins
Fold Fold foldb.18 — Galactose-binding domain-like
Superfamily Superfamily superfamilyb.18.1 — Galactose-binding domain-like
Family Family familyb.18.1.0 — automated matches
Domain ID domain_idd5dn2b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5dn2c1
Class classb — All beta proteins
Fold Fold foldb.18 — Galactose-binding domain-like
Superfamily Superfamily superfamilyb.18.1 — Galactose-binding domain-like
Family Family familyb.18.1.0 — automated matches
Domain ID domain_idd5dn2c2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5dn2d1
Class classb — All beta proteins
Fold Fold foldb.18 — Galactose-binding domain-like
Superfamily Superfamily superfamilyb.18.1 — Galactose-binding domain-like
Family Family familyb.18.1.0 — automated matches
Domain ID domain_idd5dn2d2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (4 domains)

Domain ID domain_id5dn2A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id5dn2B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id5dn2C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id5dn2D00
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)