4N19: Peptidyl-prolyl cis-trans isomerase FKBP1A

Structural basis of conformational transitions in the active site and 80 s loop in the FK506 binding protein FKBP12. Determined by X-ray diffraction at 1.2 Å resolution. Released 12 Feb 2014.

Method
X-ray diffraction
Resolution
1.2 Å
Organism
Homo sapiens
Chains
1
Atoms
1,064
Mol. weight
11.97 kDa
Released
12 Feb 2014

Explore 4N19 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4N19 contains 4 α-helices and 8 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: 4 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand2-871
α-helix201
β-strand21-2991
β-strand35-3841
β-strand46-4941
α-helix57-626
α-helix63-653
β-strand71-7661
α-helix78-803
β-strand8712
β-strand9112
β-strand97-106101

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Peptidyl-prolyl cis-trans isomerase FKBP1AAprotein107Homo sapiensP62942 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4N19_1 Peptidyl-prolyl cis-trans isomerase FKBP1A (chains A)
GVQVETISPGDGRTFPKRGQTVVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWE
EGVAQMSVGQRAKLTISPDYAYGATGHPPIIPPHATLVFDVELLKLE

Primary citation

Structural basis of conformational transitions in the active site and 80's loop in the FK506-binding protein FKBP12. Mustafi, S.M., Brecher, M., Zhang, J. et al. Biochem J (2014) 458:525-536. DOI 10.1042/BJ20131429 · PubMed

Other PDB entries of the same protein (UniProt P62942 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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