4TW8: The Fk1-Fk2 domains of FKBP52

The Fk1-Fk2 domains of FKBP52 in complex with iFit-FL. Determined by X-ray diffraction at 3.0 Å resolution. Released 26 Nov 2014.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,841
Mol. weight: 55.12 kDa
Ligands: 37M
Released: 26 Nov 2014

Explore 4TW8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4TW8 contains 18 α-helices and 38 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: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	23-24	2	1
β-strand	33-39	7	1
β-strand	42	1	2
α-helix	47-48	2
β-strand	52-61	10	1
β-strand	67-69	3	1
α-helix	76	1
β-strand	77-80	4	1
α-helix	88-94	7
β-strand	99	1	2
β-strand	102-107	6	1
α-helix	109-111	3
β-strand	118	1	3
β-strand	122	1	3
β-strand	128-138	11	1
α-helix	139	1
β-strand	140-141	2	4
β-strand	150-156	7	4
α-helix	157-158	2
β-strand	169-177	9	4
β-strand	182-191	10	4
α-helix	195-198	4
α-helix	202-208	7
β-strand	216-221	6	4
α-helix	223-225	3
β-strand	232	1	5
α-helix	233-235	3
β-strand	237	1	5
β-strand	243-253	11	4

Chain B: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	23-24	2	6
β-strand	33-39	7	6
β-strand	42	1	7
β-strand	52-61	10	6
β-strand	67-69	3	6
α-helix	76	1
β-strand	77-80	4	6
α-helix	88-94	7
β-strand	99	1	7
β-strand	102-107	6	6
α-helix	109-111	3
β-strand	118	1	8
β-strand	122	1	8
β-strand	128-138	11	6
β-strand	140-141	2	9
β-strand	150-156	7	9
α-helix	157-158	2
β-strand	169-178	10	9
β-strand	181-191	11	9
α-helix	196-198	3
α-helix	202-208	7
β-strand	216-221	6	9
α-helix	223-225	3
β-strand	232	1	10
α-helix	233-235	3
β-strand	237	1	10
β-strand	243-253	11	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase FKBP4	A, B	protein	235	Homo sapiens	Q02790 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4TW8_1 Peptidyl-prolyl cis-trans isomerase FKBP4 (chains A, B)
EGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFD
LGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSAGSPPKIPPNATLVFEVELFEFKGE
DLTEEEDGGIIRRIQTRGEGYAKPNEGAIVEVALEGYYKDKLFDQRELRFEIGEGENLDL
PYGLERAIQRMEKGEHSIVYLKPSYAFGSVGKEKFQIPPNAELKYELHLKSFEKA

Ligands and cofactors

ID	Name	Formula	Copies
37M	2-(5-{[({3-[(1R)-1-[({(2S)-1-[(2S)-2-[(1S)-cyclohex-2-en-1-yl]-2-(3,4,5-trimeth…	C63 H64 N2 O15	2

Primary citation

Selective inhibitors of the FK506-binding protein 51 by induced fit. Gaali, S., Kirschner, A., Cuboni, S. et al. Nat Chem Biol (2015) 11:33-37. DOI 10.1038/nchembio.1699 · PubMed

Other PDB entries of the same protein (UniProt Q02790 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4LAY 1.7 Å, Crystal Structure Analysis of FKBP52, Complex with I63
4DRJ 1.8 Å, o-crystal structure of the PPIase domain of FKBP52, Rapamycin and the FRB fragment of mTOR
4LAV 1.8 Å, Crystal Structure Analysis of FKBP52, Crystal Form II
1Q1C 1.9 Å, Crystal structure of N(1-260) of human FKBP52
4LAX 2.01 Å, Crystal Structure Analysis of FKBP52, Complex with FK506
6RCY 2.3 Å, Crystal structure of FK1 domain of FKBP52 in complex with a bio-inspired hybrid…
1N1A 2.4 Å, Crystal Structure of the N-terminal domain of human FKBP52
4LAW 2.4 Å, Crystal Structure Analysis of FKBP52, Crystal Form III
1P5Q 2.8 Å, Crystal Structure of FKBP52 C-terminal Domain
1QZ2 3.0 Å, Crystal Structure of FKBP52 C-terminal Domain complex with the C-terminal peptide MEEVD…
8FFV 3.01 Å, Cryo-EM structure of the GR-Hsp90-FKBP52 complex

Browse structure collections

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