2x1x

CRYSTAL STRUCTURE OF VEGF-C IN COMPLEX WITH DOMAINS 2 AND 3 OF VEGFR2 IN A TETRAGONAL CRYSTAL FORM

Method: X-RAY DIFFRACTION Dmax: 92.5 Å Quality: GOOD

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

VASCULAR ENDOTHELIAL GROWTH FACTOR C

HOMO SAPIENS

UniProt P49767

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 8 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 112–215 Fragment:VEGF HOMOLOGY DOMAIN, RESIDUES 112-215 Mutation:YES VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 × 2 (P35968) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 HG MERCURY (II) ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;100 MM NA-ACETATE BUFFER, PH 4.4-4.8, 50 MM CSCL, 28-32 % (W/V) JEFFAMINE 600 Resolution 3.10 Å R-free 0.334

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VEGFC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–104; UniProt 112–215

VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2

HOMO SAPIENS

UniProt P35968

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 8 PDB declaration: tetrameric(4) Consistent with protein copy count Chain R; UniProt 120–326 Fragment:IG-LIKE DOMAINS 2 AND 3, RESIDUES 120-326 VASCULAR ENDOTHELIAL GROWTH FACTOR C × 2 (P49767) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 HG MERCURY (II) ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;100 MM NA-ACETATE BUFFER, PH 4.4-4.8, 50 MM CSCL, 28-32 % (W/V) JEFFAMINE 600 Resolution 3.10 Å R-free 0.334

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.

53 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VGFR2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 1–207; UniProt 120–326

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 2x1x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2x1x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2x1x
Deposition date deposition_date2010-01-08
Structure title titleCRYSTAL STRUCTURE OF VEGF-C IN COMPLEX WITH DOMAINS 2 AND 3 OF VEGFR2 IN A TETRAGONAL CRYSTAL FORM
Keywords keywords;HORMONE-SIGNALING PROTEIN COMPLEX, ANGIOGENESIS, GLYCOPROTEIN, HOST-VIRUS INTERACTION, RECEPTOR, LYMPHANGIOGENESIS, IMMUNOGLOBULIN DOMAIN, DEVELOPMENTAL PROTEIN, MITOGEN ;; HORMONE/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.65
Radius of gyration Rg (electron density) rg_electron26.76
Forward intensity I(0) i022874900.00
Molecular weight molecular_weight35617.0 kDa
Excluded volume excluded_volume44242 ų
Envelope volume envelope_volume62277 ų
Hydration-shell volume shell_volume21156 ų
Envelope diameter envelope_diameter97.0
Shell Rg shell_rg31.51
Envelope Rg envelope_rg26.85
Shape Rg shape_rg26.76
Total Rg total_rg27.36
Total atoms total_atoms2476
Residues n_residues304
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 dmax92.5
Rg (real space) rg_real27.67
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real2.2870e+07
I(0) uncertainty (real space) i0_real_error3.4870e+05
Rg (reciprocal space) rg_reciprocal27.67
I(0) (reciprocal space) i0_reciprocal22870000.0000
Solution quality estimate total_estimate0.8859
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.3
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.632
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1969000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.874; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2x1xe_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id2x1xE00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id2x1xR01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2x1xR02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)