1QTY: Vascular endothelial growth factor
Vascular endothelial growth factor in complex with domain 2 of the flt-1 receptor. Determined by X-ray diffraction at 2.7 Å resolution. Released 12 Jan 2000.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 6,121
- Mol. weight
- 93.95 kDa
- Released
- 12 Jan 2000
Explore 1QTY in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1QTY contains 20 α-helices and 72 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.
Chain R: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 15 | 1 | 7 |
| α-helix | 17-24 | 8 | |
| 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 | 66-84 | 19 | 10 |
| β-strand | 87-106 | 20 | 10 |
Chain S: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14 | 1 | |
| β-strand | 15 | 1 | 10 |
| α-helix | 16 | 1 | |
| α-helix | 17-24 | 8 | |
| 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 | 66-84 | 19 | 7 |
| β-strand | 87-106 | 20 | 7 |
Chains T, U and Y: 2 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 135 | 1 | 19 |
| α-helix | 143 | 1 | |
| β-strand | 144-148 | 5 | 20 |
| β-strand | 154-156 | 3 | 21 |
| β-strand | 160 | 1 | 19 |
| β-strand | 168-171 | 4 | 20 |
| β-strand | 175-177 | 3 | 20 |
| β-strand | 184-187 | 4 | 21 |
| β-strand | 191-194 | 4 | 21 |
| α-helix | 199-201 | 3 | |
| β-strand | 204-211 | 8 | 20 |
| β-strand | 214-224 | 11 | 20 |
Chain V: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 14-15 | 2 | 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 | 13 |
| α-helix | 143 | 1 | |
| β-strand | 144-148 | 5 | 14 |
| β-strand | 154-156 | 3 | 15 |
| β-strand | 160 | 1 | 13 |
| β-strand | 168-171 | 4 | 14 |
| β-strand | 175-177 | 3 | 14 |
| α-helix | 178-179 | 2 | |
| β-strand | 184-187 | 4 | 15 |
| β-strand | 191-194 | 4 | 15 |
| α-helix | 199-201 | 3 | |
| β-strand | 204-210 | 7 | 14 |
| β-strand | 215-224 | 10 | 14 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Vascular endothelial growth factor | R, S, V, W | protein | 102 | Homo sapiens | P15692 (AlphaFold model) |
| Fms-like tyrosine kinase 1 | T, U, X, Y | protein | 101 | Homo sapiens | P17948 (AlphaFold model) |
Sequence of entity 1 (R, S, V, W), FASTA
>1QTY_1 VASCULAR ENDOTHELIAL GROWTH FACTOR (chains R, S, V, W)
GQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLE
CVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD
Sequence of entity 2 (T, U, X, Y), FASTA
>1QTY_2 FMS-LIKE TYROSINE KINASE 1 (chains T, U, X, Y)
SDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDS
RKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTI
Primary citation
Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states. Starovasnik, M.A., Christinger, H.W., Wiesmann, C. et al. J Mol Biol (1999) 293:531-544. DOI 10.1006/jmbi.1999.3134 · 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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