2qqj

Crystal Structure of the b1b2 Domains from Human Neuropilin-2

Method: X-RAY DIFFRACTION Dmax: 78.8 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 275–595 Fragment:F5/8 type C 1 and C 2 domains GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;297 K;0.1 M Bis-Tris, 20% PEG 5000 MME, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K Resolution 1.95 Å R-free 0.235

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 5–325; UniProt 275–595

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 2qqj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2qqj
Deposition date deposition_date2007-07-26
Structure title titleCrystal Structure of the b1b2 Domains from Human Neuropilin-2
Keywords keywords;VEGF receptor, semaphorin receptor, Developmental protein, Differentiation, Glycoprotein, Membrane, Neurogenesis, Transmembrane, HORMONE, 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_guinier23.00
Radius of gyration Rg (electron density) rg_electron22.07
Forward intensity I(0) i022889100.00
Molecular weight molecular_weight35604.0 kDa
Excluded volume excluded_volume44224 ų
Envelope volume envelope_volume52520 ų
Hydration-shell volume shell_volume20722 ų
Envelope diameter envelope_diameter81.6
Shell Rg shell_rg27.90
Envelope Rg envelope_rg22.29
Shape Rg shape_rg22.11
Total Rg total_rg22.70
Total atoms total_atoms2509
Residues n_residues315
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 dmax78.8
Rg (real space) rg_real23.10
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real2.2890e+07
I(0) uncertainty (real space) i0_real_error3.1470e+05
Rg (reciprocal space) rg_reciprocal23.08
I(0) (reciprocal space) i0_reciprocal22890000.0000
Solution quality estimate total_estimate0.8561
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis-0.328
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4881000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.755; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.906; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2qqja1
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_idd2qqja2
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

CATH v4.4 (2 domains)

Domain ID domain_id2qqjA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily260 — Galactose-binding domain-like
Domain ID domain_id2qqjA02
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)