5TGK: PDB entry 5TGK

Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with dATP. Determined by X-ray diffraction at 1.91 Å resolution. Released 9 May 2018.

Method: X-ray diffraction
Resolution: 1.91 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,848
Mol. weight: 26.04 kDa
Ligands: MG, DTP
Released: 9 May 2018

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

Secondary structure: helices and β-sheets

5TGK contains 11 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: 11 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	392-399	8	1
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	479-484	6	1
β-strand	488-491	4	2
β-strand	500-501	2	3
α-helix	502-507	6
α-helix	511-512	2
α-helix	514-523	10
α-helix	526-531	6
α-helix	536-538	3
β-strand	540-541	2	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	630-634	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cystic fibrosis transmembrane conductance regulator	A	protein	229	Homo sapiens	P13569 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5TGK_1 Cystic fibrosis transmembrane conductance regulator (chains A)
SLTTTEVVMENVTAFWEEGGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMMIMGELEP
SEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKD
NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMAN
KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMG

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
DTP	2'-deoxyadenosine 5'-triphosphate	C10 H16 N5 O12 P3	1

Primary citation

Ligand binding to a remote site thermodynamically corrects the F508del mutation in the human cystic fibrosis transmembrane conductance regulator. Wang, C., Aleksandrov, A.A., Yang, Z. et al. J Biol Chem (2018). DOI 10.1074/jbc.RA117.000819 · 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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