A3 domain of von willebrand factor. Determined by X-ray diffraction at 2.2 Å resolution. Released 22 Jul 1998.
Explore 1AO3 in 3D Show helices and sheets RCSB PDB PDBe
1AO3 contains 19 α-helices and 15 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 | 5-12 | 8 | 1 |
| α-helix | 20-35 | 16 | |
| β-strand | 38 | 1 | 1 |
| β-strand | 43-50 | 8 | 1 |
| β-strand | 55-58 | 4 | 1 |
| α-helix | 66-74 | 9 | |
| α-helix | 85-97 | 13 | |
| α-helix | 103-104 | 2 | |
| β-strand | 108-115 | 8 | 1 |
| α-helix | 124-132 | 9 | |
| β-strand | 135-142 | 8 | 1 |
| α-helix | 148-154 | 7 | |
| α-helix | 156-158 | 3 | |
| β-strand | 159 | 1 | 2 |
| α-helix | 160-162 | 3 | |
| β-strand | 164-166 | 3 | 1 |
| α-helix | 171-177 | 7 | |
| α-helix | 181-186 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-12 | 8 | 2 |
| α-helix | 20-35 | 16 | |
| β-strand | 38 | 1 | 2 |
| β-strand | 43-50 | 8 | 2 |
| β-strand | 54-58 | 5 | 2 |
| α-helix | 66-75 | 10 | |
| α-helix | 85-96 | 12 | |
| α-helix | 99-101 | 3 | |
| β-strand | 108-115 | 8 | 2 |
| α-helix | 124-132 | 9 | |
| β-strand | 135-142 | 8 | 2 |
| α-helix | 148-155 | 8 | |
| α-helix | 160-162 | 3 | |
| β-strand | 164-166 | 3 | 2 |
| α-helix | 171-177 | 7 | |
| α-helix | 181-186 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Von willebrand factor | A, B | protein | 187 | Homo sapiens | P04275 (AlphaFold model) |
>1AO3_1 VON WILLEBRAND FACTOR (chains A, B) CSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPW NVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTDVSV DSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMVTLGN SFLHKLC
The von willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif. Bienkowska, J., Cruz, M., Atiemo, A. et al. J Biol Chem (1997) 272:25162-25167. DOI 10.1074/jbc.272.40.25162 · PubMed
Other PDB entries of the same protein (UniProt P04275 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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