1FLT: Vegf

Vegf in complex with domain 2 of the flt-1 receptor. Determined by X-ray diffraction at 1.7 Å resolution. Released 13 Jan 1999.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,566
Mol. weight: 44.84 kDa
Released: 13 Jan 1999

Explore 1FLT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FLT contains 12 α-helices and 36 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain V: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	14	1
β-strand	15	1	1
α-helix	16	1
α-helix	17-24	8
β-strand	25	1	2
β-strand	27-34	8	3
α-helix	35-38	4
β-strand	46-48	3	4
β-strand	51-58	8	3
β-strand	60	1	2
β-strand	66-83	18	4
β-strand	89-106	18	4

Chain W: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	15	1	4
α-helix	17-24	8
β-strand	25	1	5
β-strand	27-34	8	6
α-helix	35-38	4
β-strand	46-48	3	1
β-strand	51-58	8	6
β-strand	60	1	5
β-strand	66-83	18	1
β-strand	89-106	18	1

Chain X: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	135	1	7
α-helix	138-139	2
α-helix	143	1
β-strand	144-148	5	8
β-strand	154-156	3	9
β-strand	160	1	7
β-strand	168-171	4	8
β-strand	175-177	3	8
β-strand	184-187	4	9
β-strand	191-194	4	9
α-helix	199-201	3
β-strand	203-211	9	8
β-strand	214-224	11	8

Chain Y: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	135	1	10
α-helix	138-139	2
α-helix	143	1
β-strand	144-148	5	11
β-strand	154-156	3	12
β-strand	160	1	10
β-strand	167-171	5	11
β-strand	175-177	3	11
β-strand	184-187	4	12
β-strand	191-194	4	12
α-helix	199-201	3
β-strand	204-211	8	11
β-strand	214-224	11	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vascular endothelial growth factor	V, W	protein	98	Homo sapiens	P15692 (AlphaFold model)
Fms-like tyrosine kinase 1	X, Y	protein	95	Homo sapiens	P17948 (AlphaFold model)

Sequence of entity 1 (V, W), FASTA

>1FLT_1 VASCULAR ENDOTHELIAL GROWTH FACTOR (chains V, W)
HEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPT
EESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD

Sequence of entity 2 (X, Y), FASTA

>1FLT_2 FMS-LIKE TYROSINE KINASE 1 (chains X, Y)
GRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKG
FIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQT

Primary citation

Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Wiesmann, C., Fuh, G., Christinger, H.W. et al. Cell (1997) 91:695-704. DOI 10.1016/S0092-8674(00)80456-0 · PubMed

Other PDB entries of the same protein (UniProt P15692 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1MKK 1.32 Å, Disulfide deficient mutant of vascular endothelial growth factor A (C61A and C104A)
9JU1 1.45 Å, Helix-loop-helix peptide (VS42-LR3) in complex with VEGF-A
9KKU 1.46 Å, Helix-loop-helix peptide (M49) in complex with VEGF-A
4GLN 1.6 Å, Crystal Structure of Chemically Synthesized Heterochiral {D-Protein Antagonist plus…
4GLS 1.6 Å, Crystal Structure of Chemically Synthesized Heterochiral {D-Protein Antagonist plus…
6ZBR 1.6 Å, VEGF-A 13:107 crystallized with 4C bicyclic peptide
6ZFL 1.6 Å, High resolution structure of VEGF-A 12:107 crystallized in tetragonal form
4KZN 1.71 Å, crystal structure of human VEGF-A receptor binding domain
4QAF 1.8 Å, Crystal structure of an engineered lipocalin (Anticalin) in complex with VEGF(8-109)
6Z13 1.8 Å, VEGF-A 13:107 crystallized with 3C bicyclic peptide
6ZCD 1.8 Å, VEGF-A 13:107 crystallized with 1C bicyclic peptide
3QTK 1.85 Å, The crystal structure of chemically synthesized VEGF-A

Browse structure collections

About this viewer

MolViewer shows 1FLT directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.