Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin. Determined by X-ray diffraction at 2.1 Å resolution. Released 17 Jan 2006.
Explore 1YRT in 3D Show helices and sheets RCSB PDB PDBe
1YRT contains 23 α-helices and 23 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 |
|---|---|---|---|
| α-helix | 12-16 | 5 | |
| α-helix | 21-33 | 13 | |
| β-strand | 36-41 | 6 | 1 |
| α-helix | 42-44 | 3 | |
| α-helix | 45-52 | 8 | |
| β-strand | 56-57 | 2 | 2 |
| α-helix | 65-67 | 3 | |
| α-helix | 70-72 | 3 | |
| β-strand | 77 | 1 | 3 |
| α-helix | 80-82 | 3 | |
| α-helix | 90-105 | 16 | |
| β-strand | 109-112 | 4 | 3 |
| β-strand | 114-115 | 2 | 4 |
| α-helix | 117-125 | 9 | |
| β-strand | 131-132 | 2 | 5 |
| β-strand | 136 | 1 | 4 |
| β-strand | 137-138 | 2 | 5 |
| α-helix | 142-145 | 4 | |
| β-strand | 147-153 | 7 | 4 |
| β-strand | 159-165 | 7 | 4 |
| β-strand | 172-173 | 2 | 4 |
| α-helix | 174 | 1 | |
| β-strand | 175-178 | 4 | 3 |
| β-strand | 184 | 1 | 3 |
| β-strand | 185-186 | 2 | 2 |
| β-strand | 191-196 | 6 | 1 |
| β-strand | 197 | 1 | 6 |
| α-helix | 198-201 | 4 | |
| α-helix | 202-209 | 8 | |
| α-helix | 215-222 | 8 | |
| α-helix | 235-252 | 18 | |
| α-helix | 257-259 | 3 | |
| β-strand | 262-264 | 3 | 7 |
| β-strand | 267-270 | 4 | 7 |
| α-helix | 274-289 | 16 | |
| α-helix | 301-303 | 3 | |
| β-strand | 313-316 | 4 | 1 |
| β-strand | 322-325 | 4 | 1 |
| α-helix | 327-339 | 13 | |
| β-strand | 342 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 82-92 | 11 | |
| β-strand | 99-100 | 2 | 8 |
| α-helix | 102-111 | 10 | |
| α-helix | 118-128 | 11 | |
| β-strand | 136-137 | 2 | 8 |
| α-helix | 138-146 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bifunctional hemolysin-adenylate cyclase | A | protein | 364 | Bordetella pertussis | P0DKX7 (AlphaFold model) |
| Calmodulin | B | protein | 74 | Homo sapiens | P0DP23 (AlphaFold model) |
>1YRT_1 Bifunctional hemolysin-adenylate cyclase (chains A) MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGL GVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERL DYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNA AGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDL LWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGT EQNNPFPEADEKIFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDD GLGA
>1YRT_2 Calmodulin (chains B) KMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDG QVNYEEFVQMMTAK
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 2 |
Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin. Guo, Q., Shen, Y., Lee, Y.S. et al. EMBO J (2005) 24:3190-3201. DOI 10.1038/sj.emboj.7600800 · PubMed
Other PDB entries of the same protein (UniProt P0DKX7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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