structure of platelet Glycoprotein 1b alpha with a bound peptide inhibitor. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Nov 2010.
Explore 3P72 in 3D Show helices and sheets RCSB PDB PDBe
3P72 contains 11 α-helices and 18 β-strands across 2 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 | 5-9 | 5 | 1 |
| β-strand | 12-16 | 5 | 1 |
| β-strand | 35-37 | 3 | 1 |
| β-strand | 45-47 | 3 | 2 |
| α-helix | 48-51 | 4 | |
| β-strand | 59-61 | 3 | 1 |
| β-strand | 69-71 | 3 | 2 |
| β-strand | 81-83 | 3 | 1 |
| β-strand | 104-106 | 3 | 1 |
| β-strand | 128-130 | 3 | 1 |
| β-strand | 152-154 | 3 | 1 |
| β-strand | 176-178 | 3 | 1 |
| β-strand | 199-201 | 3 | 1 |
| β-strand | 207 | 1 | 3 |
| α-helix | 211-213 | 3 | |
| α-helix | 214-222 | 9 | |
| α-helix | 224-226 | 3 | |
| β-strand | 227-228 | 2 | 1 |
| α-helix | 236-238 | 3 | |
| α-helix | 240 | 1 | |
| β-strand | 241 | 1 | 1 |
| α-helix | 243-245 | 3 | |
| β-strand | 247 | 1 | 4 |
| β-strand | 248 | 1 | 3 |
| β-strand | 255 | 1 | 4 |
| α-helix | 256-258 | 3 | |
| α-helix | 264 | 1 | |
| α-helix | 266 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-8 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Platelet glycoprotein Ib alpha chain | A | protein | 269 | Homo sapiens | P07359 (AlphaFold model) |
| OS1 peptide | B | protein | 11 |
>3P72_1 Platelet glycoprotein Ib alpha chain (chains A) HPICEVSKVASHLEVNCDKRQLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQL NLDRCELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGAL RGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNQLTELPAGLLNGLENLDTLLLQ ENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQGVDVKAMT SNVASVQCDNSDKFPVYKYPGKGCPLVPR
>3P72_2 OS1 peptide (chains B) CTERMALHNLC
Glycoprotein Ibalpha inhibitor complex structure reveals a combined steric and allosteric mechanism of von Willebrand factor antagonism. McEwan, P.A., Andrews, R.K., Emsley, J. Blood (2009) 114:4883-4885. DOI 10.1182/blood-2009-05-224170 · PubMed
Other PDB entries of the same protein (UniProt P07359 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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