Crystal Structure of Chemically Synthesized Heterochiral {D-Protein Antagonist plus VEGF-A} Protein Complex in space group P21/n. Determined by X-ray diffraction at 1.6 Å resolution. Released 5 Sept 2012.
Explore 4GLN in 3D Show helices and sheets RCSB PDB PDBe
4GLN contains 11 α-helices and 26 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 |
|---|---|---|---|
| β-strand | 2-7 | 6 | 1 |
| β-strand | 12-17 | 6 | 1 |
| α-helix | 22-36 | 15 | |
| β-strand | 39-40 | 2 | 2 |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 51-55 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7 | 1 | |
| β-strand | 8 | 1 | 2 |
| α-helix | 9 | 1 | |
| α-helix | 10-17 | 8 | |
| β-strand | 18 | 1 | 3 |
| β-strand | 20-27 | 8 | 4 |
| α-helix | 28-31 | 4 | |
| β-strand | 39-41 | 3 | 5 |
| β-strand | 44-51 | 8 | 4 |
| β-strand | 53 | 1 | 3 |
| β-strand | 59-77 | 19 | 5 |
| β-strand | 81-99 | 19 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 8 |
| β-strand | 12-17 | 6 | 8 |
| α-helix | 22-36 | 15 | |
| β-strand | 39-40 | 2 | 5 |
| β-strand | 42-46 | 5 | 8 |
| α-helix | 47-49 | 3 | |
| β-strand | 51-55 | 5 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| D-RFX001 | D, H | protein | 56 | synthetic construct | |
| Vascular endothelial growth factor A | E, F | protein | 102 | Homo sapiens | P15692 (AlphaFold model) |
>4GLN_1 D-RFX001 (chains D, H) TYKLILNGKTLKGETTTEAVDVFDAFDVFFVYAASNFSDFDDWTYDDATKTFTVTE
>4GLN_2 Vascular endothelial growth factor A (chains E, F) GQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLE CVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD
Chemical synthesis and X-ray structure of a heterochiral {D-protein antagonist plus vascular endothelial growth factor} protein complex by racemic crystallography. Mandal, K., Uppalapati, M., Ault-Riche, D. et al. Proc Natl Acad Sci U S A (2012) 109:14779-14784. DOI 10.1073/pnas.1210483109 · 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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