1VPP: Protein

Complex between vegf and a receptor blocking peptide. Determined by X-ray diffraction at 1.9 Å resolution. Released 23 Feb 1999.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,186
Mol. weight: 28.41 kDa
Released: 23 Feb 1999

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

Secondary structure: helices and β-sheets

1VPP contains 8 α-helices and 22 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: 1 helix, 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
β-strand	46-48	3	1
β-strand	51-58	8	6
β-strand	60	1	5
β-strand	66-84	19	1
β-strand	88-106	19	1

Chain X: 2 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	4
β-strand	9	1	7
α-helix	14	1
β-strand	15	1	7
α-helix	16-18	3

Chain Y: 1 helix, 3 β-strands

Element	Residues	Length	Sheet
α-helix	3	1
β-strand	4-8	5	1
β-strand	9	1	8
β-strand	15	1	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (vascular endothelial growth factor)	V, W	protein	102	Homo sapiens	P15692 (AlphaFold model)
Protein (peptide V108)	X, Y	protein	20

Sequence of entity 1 (V, W), FASTA

>1VPP_1 PROTEIN (VASCULAR ENDOTHELIAL GROWTH FACTOR) (chains V, W)
GQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLE
CVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD

Sequence of entity 2 (X, Y), FASTA

>1VPP_2 PROTEIN (PEPTIDE V108) (chains X, Y)
RGWVEICAADDYGRCLTEAQ

Primary citation

Crystal structure of the complex between VEGF and a receptor-blocking peptide. Wiesmann, C., Christinger, H.W., Cochran, A.G. et al. Biochemistry (1998) 37:17765-17772. DOI 10.1021/bi9819327 · 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
1FLT 1.7 Å, Vegf in complex with domain 2 of the flt-1 receptor
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

Browse structure collections

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