2BBS: PDB entry 2BBS

Human deltaF508 NBD1 with three solubilizing mutations. Determined by X-ray diffraction at 2.05 Å resolution. Released 1 Nov 2005.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,202
Mol. weight: 65.83 kDa
Ligands: ATP, MG
Released: 1 Nov 2005

Explore 2BBS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 16 helices, 11 β-strands

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

Chain B: 13 helices, 13 β-strands

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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cystic fibrosis transmembrane conductance regulator	A, B	protein	290	Homo sapiens	P13569 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2BBS_1 Cystic fibrosis transmembrane conductance regulator (chains A, B)
STTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLSFSNFSLLGTPVLKDINFK
IERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQNSWIMPGTIKENII
GVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADL
YLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG
TFSELQNLRPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVS

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
MG	Magnesium ion	Mg	2

Primary citation

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:

2PZE 1.7 Å, Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer
7QI1 1.76 Å, Crystal structure of human 14-3-3 protein beta in complex with CFTR peptide pS753pS768…
2PZG 1.8 Å, Minimal human CFTR first nucleotide binding domain as a monomer
5TFJ 1.85 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
6WBS 1.86 Å, Human CFTR first nucleotide binding domain with dF508/V510D
6HEP 1.86 Å, Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768
5TF8 1.86 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFA 1.87 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFB 1.87 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFD 1.89 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFF 1.89 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…
5TFI 1.89 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…

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