1flt

VEGF IN COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR

Method: X-RAY DIFFRACTION Dmax: 95.7 Å Quality: GOOD

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

VASCULAR ENDOTHELIAL GROWTH FACTOR

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain V; UniProt 38–135 Chain W; UniProt 38–135 Fragment:RECEPTOR BINDING DOMAIN, RESIDUES 8 - 109 FMS-LIKE TYROSINE KINASE 1 × 2 (P17948) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;pH 8.5 Resolution 1.70 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain V; UniProt 38–135 Chain W; UniProt 38–135 Fragment:RECEPTOR BINDING DOMAIN, RESIDUES 8 - 109 FMS-LIKE TYROSINE KINASE 1 × 4 (P17948) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;pH 8.5 Resolution 1.70 Å R-free 0.261

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 71 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VEGFA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain V; PDBConstruct 1–98; UniProt 38–135 Author chain W; PDBConstruct 1–98; UniProt 38–135

FMS-LIKE TYROSINE KINASE 1

Homo sapiens

UniProt P17948

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain X; UniProt 132–226 Chain Y; UniProt 132–226 Fragment:SECOND EXTRACELLULAR IGG LIKE DOMAIN, RESIDUES 129 - 229 VASCULAR ENDOTHELIAL GROWTH FACTOR × 2 (P15692) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;pH 8.5 Resolution 1.70 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain X; UniProt 132–226 Chain Y; UniProt 132–226 Fragment:SECOND EXTRACELLULAR IGG LIKE DOMAIN, RESIDUES 129 - 229 VASCULAR ENDOTHELIAL GROWTH FACTOR × 4 (P15692) X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;pH 8.5 Resolution 1.70 Å R-free 0.261

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.

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

View Construct and Data Evidence
UniProt name VGFR1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain X; PDBConstruct 1–95; UniProt 132–226 Author chain Y; PDBConstruct 1–95; UniProt 132–226

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 1flt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1flt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1flt
Deposition date deposition_date1997-11-20
Structure title titleVEGF IN COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR
Keywords keywords;COMPLEX (GROWTH FACTOR-TRANSFERASE), FLT-1 RECEPTOR, CYSTINE KNOT, GLYCOPROTEIN, IMMUNOGLOBULIN-LIKE DOMAIN TRANSFERASE, COMPLEX (GROWTH FACTOR-TRANSFERASE) complex ;; COMPLEX (GROWTH FACTOR/TRANSFERASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.22
Radius of gyration Rg (electron density) rg_electron28.02
Forward intensity I(0) i032746800.00
Molecular weight molecular_weight44218.0 kDa
Excluded volume excluded_volume55268 ų
Envelope volume envelope_volume72959 ų
Hydration-shell volume shell_volume22990 ų
Envelope diameter envelope_diameter100.4
Shell Rg shell_rg33.39
Envelope Rg envelope_rg27.89
Shape Rg shape_rg28.07
Total Rg total_rg28.45
Total atoms total_atoms3090
Residues n_residues382
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 dmax95.7
Rg (real space) rg_real28.50
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real3.2750e+07
I(0) uncertainty (real space) i0_real_error5.4810e+05
Rg (reciprocal space) rg_reciprocal28.42
I(0) (reciprocal space) i0_reciprocal32740000.0000
Solution quality estimate total_estimate0.8480
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.490
Kurtosis Kurtosis kurtosis-0.454
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4264000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.709; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1fltv_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.1 — Platelet-derived growth factor-like
Domain ID domain_idd1fltw_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.1 — Platelet-derived growth factor-like
Domain ID domain_idd1fltx_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains
Domain ID domain_idd1flty_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains

CATH v4.4 (4 domains)

Domain ID domain_id1fltV00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id1fltW00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id1fltX00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1fltY00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)