Human deltaF508 NBD1 with three solubilizing mutations. Determined by X-ray diffraction at 2.05 Å resolution. Released 1 Nov 2005.
Explore 2BBS in 3D Show helices and sheets RCSB PDB PDBe
2BBS contains 29 α-helices and 24 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 | 392-399 | 8 | 1 |
| α-helix | 403-411 | 9 | |
| β-strand | 441-448 | 8 | 1 |
| α-helix | 452 | 1 | |
| β-strand | 453-458 | 6 | 2 |
| α-helix | 464-471 | 8 | |
| β-strand | 477-483 | 7 | 1 |
| β-strand | 488-491 | 4 | 2 |
| β-strand | 501 | 1 | 3 |
| α-helix | 502-507 | 6 | |
| α-helix | 514-523 | 10 | |
| α-helix | 527-531 | 5 | |
| α-helix | 536-538 | 3 | |
| β-strand | 540 | 1 | 3 |
| α-helix | 547-549 | 3 | |
| α-helix | 550-563 | 14 | |
| β-strand | 568-572 | 5 | 2 |
| α-helix | 580-586 | 7 | |
| α-helix | 587-594 | 8 | |
| β-strand | 599-603 | 5 | 2 |
| α-helix | 607-612 | 6 | |
| β-strand | 615-620 | 6 | 2 |
| β-strand | 623-628 | 6 | 2 |
| α-helix | 630-636 | 7 | |
| α-helix | 638-644 | 7 | |
| α-helix | 650-652 | 3 | |
| α-helix | 655-669 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 392-399 | 8 | 4 |
| β-strand | 441 | 1 | 4 |
| β-strand | 442 | 1 | 5 |
| β-strand | 443-448 | 6 | 4 |
| β-strand | 453-458 | 6 | 5 |
| α-helix | 464-471 | 8 | |
| β-strand | 477-483 | 7 | 4 |
| β-strand | 488-491 | 4 | 5 |
| β-strand | 500-501 | 2 | 6 |
| α-helix | 502-507 | 6 | |
| α-helix | 514-523 | 10 | |
| α-helix | 527-530 | 4 | |
| α-helix | 536-538 | 3 | |
| β-strand | 540-541 | 2 | 6 |
| α-helix | 547-549 | 3 | |
| α-helix | 550-563 | 14 | |
| β-strand | 568-572 | 5 | 5 |
| α-helix | 580-586 | 7 | |
| α-helix | 587-594 | 8 | |
| β-strand | 599-603 | 5 | 5 |
| α-helix | 607-612 | 6 | |
| β-strand | 615-620 | 6 | 5 |
| β-strand | 623-628 | 6 | 5 |
| α-helix | 630-636 | 7 | |
| α-helix | 650-652 | 3 | |
| α-helix | 655-668 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cystic fibrosis transmembrane conductance regulator | A, B | protein | 290 | Homo sapiens | P13569 (AlphaFold model) |
>2BBS_1 Cystic fibrosis transmembrane conductance regulator (chains A, B) STTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLSFSNFSLLGTPVLKDINFK IERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQNSWIMPGTIKENII GVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADL YLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG TFSELQNLRPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVS
Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry. Lewis, H.A., Wang, C., Zhao, X. et al. J Mol Biol (2010) 396:406-430. DOI 10.1016/j.jmb.2009.11.051 · PubMed
Other PDB entries of the same protein (UniProt P13569 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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