5CXL: Bifunctional hemolysin/adenylate cyclase

Crystal structure of rtx domain block V of adenylate cyclase toxin from bordetella pertussis. Determined by X-ray diffraction at 1.45 Å resolution. Released 2 Sept 2015.

Method
X-ray diffraction
Resolution
1.45 Å
Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Chains
2
Atoms
2,582
Mol. weight
32.81 kDa
Ligands
CA
Released
2 Sept 2015

Explore 5CXL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CXL contains 6 α-helices and 28 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.

Chain A: 3 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand1535-153731
β-strand1544-154632
β-strand1553-155531
β-strand1562-156432
β-strand1571-157331
β-strand1580-158452
β-strand1589-159351
β-strand1598-160362
β-strand1610-161451
α-helix1617-16193
β-strand1620-162562
β-strand1628-163362
β-strand1639-164242
α-helix1649-16513
β-strand1655-165841
β-strand1661-166441
α-helix1665-167511
Chain B: 3 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand1535-153733
β-strand1544-154634
β-strand1553-155533
β-strand1562-156434
β-strand1571-157333
β-strand1580-158454
β-strand1589-159243
β-strand1598-160364
β-strand1610-161343
α-helix1617-16193
β-strand1620-162564
β-strand1628-163364
β-strand1639-164244
α-helix1649-16513
β-strand1655-165733
β-strand1662-166323
α-helix1665-167511

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Bifunctional hemolysin/adenylate cyclaseA, Bprotein153Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)P0DKX7 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5CXL_1 Bifunctional hemolysin/adenylate cyclase (chains A, B)
GSARDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDD
TYLFGVGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRD
ADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDP

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa16

Water and common crystallization additives (NO3) are not listed.

Primary citation

Calcium-Driven Folding of RTX Domain beta-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. Bumba, L., Masin, J., Macek, P. et al. Mol Cell (2016) 62:47-62. DOI 10.1016/j.molcel.2016.03.018 · PubMed

Other PDB entries of the same protein (UniProt P0DKX7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 5CXL directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.