6WBS: PDB entry 6WBS

Human CFTR first nucleotide binding domain with dF508/V510D. Determined by X-ray diffraction at 1.86 Å resolution. Released 7 Apr 2021.

Method: X-ray diffraction
Resolution: 1.86 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,985
Mol. weight: 51.39 kDa
Ligands: MG, ATP
Released: 7 Apr 2021

Explore 6WBS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6WBS contains 24 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: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	422-431	10	1
β-strand	441	1	1
β-strand	442	1	2
β-strand	443-449	7	1
β-strand	453-458	6	2
α-helix	464-471	8
β-strand	479-483	5	1
β-strand	486	1	3
β-strand	488-491	4	2
β-strand	500-501	2	4
α-helix	502-507	6
α-helix	514-523	10
α-helix	526-531	6
α-helix	536-538	3
α-helix	539	1
β-strand	540-541	2	4
α-helix	546-549	4
α-helix	550-563	14
β-strand	568-572	5	2
α-helix	580-586	7
α-helix	587-594	8
β-strand	600-603	4	2
α-helix	607-610	4
β-strand	615-620	6	2
β-strand	623-628	6	2
α-helix	630-634	5

Chain B: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	422-431	10	5
β-strand	441	1	5
β-strand	442	1	6
β-strand	443-449	7	5
β-strand	453-457	5	6
α-helix	464-472	9
β-strand	479-484	6	5
β-strand	486	1	3
β-strand	488-491	4	6
β-strand	500-501	2	7
α-helix	502-507	6
α-helix	514-523	10
α-helix	527-531	5
α-helix	536-538	3
β-strand	540-541	2	7
α-helix	543-545	3
α-helix	550-563	14
β-strand	568-572	5	6
α-helix	580-586	7
α-helix	587-594	8
β-strand	600-603	4	6
α-helix	607-612	6
β-strand	615-620	6	6
β-strand	623-628	6	6
α-helix	630-636	7
α-helix	640-644	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cystic fibrosis transmembrane conductance regulator	A, B	protein	226	Homo sapiens	P13569 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6WBS_1 Cystic fibrosis transmembrane conductance regulator (chains A, B)
TTTEVVMENVTAFWEEGGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSE
GKIKHSGRISFCSQFSWIMPGTIKENIIGDSYDEYRYRSVIKACQLEEDISKFAEKDNIV
LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTR
ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMG

Ligands and cofactors

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

Primary citation

Determining the Molecular Mechanism of Suppressor Mutation V510D and the Contribution of Helical Unraveling to the dF508-CFTR Defect. Simon, K.S., Nagarajan, K., Mechin, I. et al. To be published.

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…
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…
5TFG 1.91 Å, Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance…

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