Crystal Structure of Chemically Synthesized Heterochiral {RFX037 plus VEGF-A} Protein Complex in space group P21/n. Determined by X-ray diffraction at 2.1 Å resolution. Released 9 Mar 2016.
Explore 5HHC in 3D Show helices and sheets RCSB PDB PDBe
5HHC contains 11 α-helices and 24 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7 | 1 | |
| β-strand | 8 | 1 | 1 |
| α-helix | 9 | 1 | |
| α-helix | 10-17 | 8 | |
| β-strand | 18 | 1 | 2 |
| β-strand | 20-27 | 8 | 3 |
| α-helix | 28-31 | 4 | |
| β-strand | 39-41 | 3 | 4 |
| β-strand | 44-51 | 8 | 3 |
| β-strand | 53 | 1 | 2 |
| β-strand | 59-77 | 19 | 4 |
| β-strand | 81-99 | 19 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-15 | 8 | 1 |
| β-strand | 20-27 | 8 | 1 |
| α-helix | 30-42 | 13 | |
| β-strand | 47-54 | 8 | 1 |
| β-strand | 59-64 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-15 | 8 | 4 |
| β-strand | 20-27 | 8 | 4 |
| α-helix | 30-44 | 15 | |
| β-strand | 47-54 | 8 | 4 |
| α-helix | 55-57 | 3 | |
| β-strand | 59-64 | 6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vascular endothelial growth factor A | A, B | protein | 102 | Homo sapiens | P15692 (AlphaFold model) |
| D- Vascular endothelial growth factor-A | C, D | protein | 69 | synthetic construct |
>5HHC_1 Vascular endothelial growth factor A (chains A, B) GQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLE CVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD
>5HHC_2 D- Vascular endothelial growth factor-A (chains C, D) RRRRRGGSTYKLILNGKTLKGETTTEAVDVFDAFDVFFVYAASNFSDFDDWTYDDATKTF TVTEGGSDK
A Potent d-Protein Antagonist of VEGF-A is Nonimmunogenic, Metabolically Stable, and Longer-Circulating in Vivo. Uppalapati, M., Lee, D.J., Mandal, K. et al. ACS Chem Biol (2016) 11:1058-1065. DOI 10.1021/acschembio.5b01006 · PubMed
Other PDB entries of the same protein (UniProt P15692 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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