2VPF: Vascular endothelial growth factor
Vascular endothelial growth factor refined to 1.93 Å resolution. Determined by X-ray diffraction at 1.93 Å resolution. Released 29 Jul 1998.
- Method
- X-ray diffraction
- Resolution
- 1.93 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 6,782
- Mol. weight
- 95.59 kDa
- Released
- 29 Jul 1998
Explore 2VPF in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2VPF contains 28 α-helices and 64 β-strands across 8 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.
Chains A, B and G: 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 C: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 15 | 1 | 7 |
| α-helix | 17-23 | 7 | |
| β-strand | 25 | 1 | 8 |
| β-strand | 27-34 | 8 | 9 |
| α-helix | 35-38 | 4 | |
| β-strand | 46-48 | 3 | 10 |
| β-strand | 51-58 | 8 | 9 |
| β-strand | 60 | 1 | 8 |
| β-strand | 67-84 | 18 | 10 |
| β-strand | 88-105 | 18 | 10 |
Chain D: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14 | 1 | |
| β-strand | 15 | 1 | 10 |
| α-helix | 16 | 1 | |
| α-helix | 17-23 | 7 | |
| β-strand | 25 | 1 | 11 |
| β-strand | 27-34 | 8 | 12 |
| α-helix | 35-38 | 4 | |
| β-strand | 46-48 | 3 | 7 |
| β-strand | 51-58 | 8 | 12 |
| β-strand | 60 | 1 | 11 |
| β-strand | 66-83 | 18 | 7 |
| β-strand | 89-106 | 18 | 7 |
Chain E: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14 | 1 | |
| β-strand | 15 | 1 | 13 |
| α-helix | 16 | 1 | |
| α-helix | 17-24 | 8 | |
| β-strand | 25 | 1 | 14 |
| β-strand | 27-34 | 8 | 15 |
| α-helix | 35-38 | 4 | |
| β-strand | 46-48 | 3 | 16 |
| β-strand | 51-58 | 8 | 15 |
| β-strand | 60 | 1 | 14 |
| β-strand | 66-84 | 19 | 16 |
| β-strand | 88-106 | 19 | 16 |
Chain F: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14 | 1 | |
| β-strand | 15 | 1 | 16 |
| α-helix | 16 | 1 | |
| α-helix | 17-24 | 8 | |
| β-strand | 25 | 1 | 17 |
| β-strand | 27-34 | 8 | 18 |
| α-helix | 35-38 | 4 | |
| β-strand | 46-48 | 3 | 13 |
| β-strand | 51-58 | 8 | 18 |
| β-strand | 60 | 1 | 17 |
| β-strand | 66-83 | 18 | 13 |
| β-strand | 90-106 | 17 | 13 |
Chain H: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 15 | 1 | 22 |
| α-helix | 17-24 | 8 | |
| β-strand | 25 | 1 | 23 |
| β-strand | 27-34 | 8 | 24 |
| α-helix | 35-38 | 4 | |
| β-strand | 46-48 | 3 | 19 |
| β-strand | 51-58 | 8 | 24 |
| β-strand | 60 | 1 | 23 |
| β-strand | 66-83 | 18 | 19 |
| β-strand | 89-106 | 18 | 19 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Vascular endothelial growth factor | A, B, C, D, E, F, G, H | protein | 102 | Homo sapiens | P15692 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>2VPF_1 VASCULAR ENDOTHELIAL GROWTH FACTOR (chains A, B, C, D, E, F, G, H)
GQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLE
CVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD
Primary citation
The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding. Muller, Y.A., Christinger, H.W., Keyt, B.A. et al. Structure (1997) 5:1325-1338. DOI 10.1016/S0969-2126(97)00284-0 · 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
- 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
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