Crystal structure of Glycoprotein VI in complex with collagen-peptide (GPO)5. Determined by X-ray diffraction at 2.5 Å resolution. Released 5 Sept 2018.
Explore 5OU8 in 3D Show helices and sheets RCSB PDB PDBe
5OU8 contains 14 α-helices and 37 β-strands across 5 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 | 4-8 | 5 | |
| β-strand | 9-13 | 5 | 1 |
| β-strand | 17-19 | 3 | 2 |
| β-strand | 24-29 | 6 | 1 |
| β-strand | 36-41 | 6 | 3 |
| β-strand | 47-48 | 2 | 3 |
| β-strand | 52-55 | 4 | 1 |
| α-helix | 60-62 | 3 | |
| β-strand | 64-72 | 9 | 3 |
| β-strand | 75-76 | 2 | 3 |
| α-helix | 77-82 | 6 | |
| β-strand | 83-85 | 3 | 3 |
| β-strand | 86-88 | 3 | 2 |
| β-strand | 95-100 | 6 | 4 |
| β-strand | 105-111 | 7 | 4 |
| β-strand | 118-123 | 6 | 5 |
| α-helix | 128 | 1 | |
| β-strand | 129-133 | 5 | 5 |
| β-strand | 137-141 | 5 | 4 |
| α-helix | 143-144 | 2 | |
| β-strand | 146-153 | 8 | 5 |
| β-strand | 160 | 1 | 2 |
| β-strand | 161 | 1 | 5 |
| α-helix | 162-167 | 6 | |
| β-strand | 168-170 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-13 | 5 | 6 |
| β-strand | 17-19 | 3 | 7 |
| β-strand | 24-29 | 6 | 6 |
| β-strand | 36-41 | 6 | 8 |
| β-strand | 46-48 | 3 | 8 |
| β-strand | 52-55 | 4 | 6 |
| α-helix | 60-62 | 3 | |
| β-strand | 64-72 | 9 | 8 |
| β-strand | 75-76 | 2 | 8 |
| α-helix | 77-82 | 6 | |
| β-strand | 83-85 | 3 | 8 |
| β-strand | 86-88 | 3 | 7 |
| β-strand | 95-100 | 6 | 9 |
| β-strand | 106-111 | 6 | 9 |
| β-strand | 118-123 | 6 | 10 |
| α-helix | 128 | 1 | |
| β-strand | 129-133 | 5 | 10 |
| β-strand | 137-140 | 4 | 9 |
| α-helix | 143-145 | 3 | |
| β-strand | 146-154 | 9 | 10 |
| β-strand | 157-161 | 5 | 10 |
| α-helix | 162-167 | 6 | |
| β-strand | 168-170 | 3 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-14 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-9 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-14 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Platelet glycoprotein VI | A, B | protein | 181 | Homo sapiens | Q9HCN6 (AlphaFold model) |
| (GPO)5 | C, D, E | protein | 15 | Homo sapiens | P02452 (AlphaFold model) |
>5OU8_1 Platelet glycoprotein VI (chains A, B) GSQSGPLPKPSLQALPSSLVPLEKPVTLRCQGPPGVDLYRLEKLSSSRYQDQAVLFIPAM KRSLAGRYRCSYQNGSLWSLPSDQLELVATGVFAKPSLSAQPGSGGDVTLQCQTRYGFDQ FALYKEGDPERWYRASFPIITVTAAHSGTYRCYSFSSRDPYLWSAPSDPLELVVTGTSAA A
>5OU8_2 (GPO)5 (chains C, D, E) GPPGPPGPPGPPGPP
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (CL, PG4) are not listed.
Structural insights into collagen binding by platelet receptor glycoprotein VI. Feitsma, L.J., Brondijk, H.C., Jarvis, G.E. et al. Blood (2022) 139:3087-3098. DOI 10.1182/blood.2021013614 · PubMed
Other PDB entries of the same protein (UniProt Q9HCN6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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