2PZG: PDB entry 2PZG

Minimal human CFTR first nucleotide binding domain as a monomer. Determined by X-ray diffraction at 1.8 Å resolution. Released 9 Oct 2007.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
2
Atoms
3,694
Mol. weight
55.47 kDa
Ligands
ATP, MG
Released
9 Oct 2007

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

Secondary structure: helices and β-sheets

2PZG contains 28 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: 14 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand392-39981
β-strand44111
β-strand44212
β-strand443-44861
β-strand453-45752
α-helix464-4718
β-strand479-48461
β-strand48613
β-strand488-49142
β-strand500-50124
α-helix502-5076
α-helix511-5122
α-helix514-52310
α-helix527-5315
α-helix536-5383
α-helix5391
β-strand540-54124
α-helix5421
α-helix550-56314
β-strand568-57252
α-helix580-5867
α-helix587-5948
β-strand600-60342
α-helix607-6126
β-strand615-62062
β-strand623-62862
α-helix630-6345
α-helix640-6445
Chain B: 14 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand392-39985
α-helix438-4392
β-strand44115
β-strand44216
β-strand443-44865
β-strand453-45756
α-helix464-4718
β-strand477-48375
β-strand48613
β-strand488-49146
β-strand500-50127
α-helix502-5076
α-helix511-5122
α-helix514-52310
α-helix527-5304
α-helix536-5383
α-helix5391
β-strand540-54127
α-helix547-5493
α-helix550-56314
β-strand568-57256
α-helix580-5867
α-helix587-5948
β-strand599-60356
α-helix607-6126
β-strand615-62066
β-strand623-62866
α-helix630-6345

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cystic fibrosis transmembrane conductance regulatorA, Bprotein241Homo sapiensP13569 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2PZG_1 Cystic fibrosis transmembrane conductance regulator (chains A, B)
SLQKQEYKTLEYNLTTTEVVMENVTAFWEEGGTPVLKDINFKIERGQLLAVAGSTGAGKT
SLLMMIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQ
LEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKE
IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLM
G

Ligands and cofactors

IDNameFormulaCopies
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32
MGMagnesium ionMg2

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant. Atwell, S., Brouillette, C.G., Conners, K. et al. Protein Eng Des Sel (2010) 23:375-384. DOI 10.1093/protein/gzq004 · 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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