4WZ6: PDB entry 4WZ6

Human CFTR aa389-678 (NBD1), deltaF508 with three solubilizing mutations, bound ATP. Determined by X-ray diffraction at 2.05 Å resolution. Released 11 Nov 2015.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,106
Mol. weight: 32.92 kDa
Ligands: ATP, MG
Released: 11 Nov 2015

Explore 4WZ6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4WZ6 contains 14 α-helices and 13 β-strands across 1 chain. 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: 14 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	392-399	8	1
α-helix	403-413	11
β-strand	441	1	1
β-strand	442	1	2
β-strand	443-448	6	1
β-strand	453-458	6	2
α-helix	464-471	8
β-strand	479-483	5	1
β-strand	488-491	4	2
β-strand	501	1	3
α-helix	502-506	5
α-helix	513-522	10
α-helix	525-530	6
α-helix	535-537	3
β-strand	539	1	3
α-helix	549-562	14
β-strand	567-571	5	2
α-helix	579-585	7
α-helix	586-593	8
β-strand	599-602	4	2
α-helix	606-611	6
β-strand	614-619	6	2
β-strand	622-627	6	2
α-helix	629-635	7
α-helix	637-643	7
α-helix	649-651	3
α-helix	654-667	14

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>4WZ6_1 Cystic fibrosis transmembrane conductance regulator (chains A)
STTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLSFSNFSLLGTPVLKDINFK
IERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQNSWIMPGTIKENII
GVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADL
YLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG
TFSELQNLRPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVS

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
MG	Magnesium ion	Mg	1

Primary citation

Binding screen for cystic fibrosis transmembrane conductance regulator correctors finds new chemical matter and yields insights into cystic fibrosis therapeutic strategy. Hall, J.D., Wang, H., Byrnes, L.J. et al. Protein Sci (2016) 25:360-373. DOI 10.1002/pro.2821 · 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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