9LYG: FKBP12

Crystal structure of FKBP12 complexed with Small Molecule Anchor for Protein-201. Determined by X-ray diffraction at 1.26 Å resolution. Released 26 Mar 2025.

Method
X-ray diffraction
Resolution
1.26 Å
Organism
Homo sapiens
Chains
1
Atoms
1,181
Mol. weight
12.91 kDa
Ligands
A1L7S
Released
26 Mar 2025

Explore 9LYG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9LYG 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-strand21-30101
β-strand35-3841
α-helix40-423
β-strand46-4941
α-helix57-648
β-strand71-7661
α-helix78-803
β-strand8712
β-strand9112
β-strand97-106101

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Peptidyl-prolyl cis-trans isomerase FKBP1AAprotein111Homo sapiensP62942 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9LYG_1 Peptidyl-prolyl cis-trans isomerase FKBP1A (chains A)
GSHMGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVI
RGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE

Ligands and cofactors

IDNameFormulaCopies
A1L7S5-[(2~{S})-1-cyclohexylsulfonylpiperidin-2-yl]-3-[3-(3,4-dimethoxyphenyl)propyl…C24 H35 N3 O5 S1

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

Primary citation

Crystal structure of FKBP12 complexed with Small Molecule Anchor for Protein-201. Kato, S., Tsuchikawa, H., Katoh, A. et al. To be published.

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

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