4LAX: Peptidyl-prolyl cis-trans isomerase FKBP4

Name: PDB 4LAX: Crystal Structure Analysis of FKBP52, Complex with FK506
Published: 2013-08-21
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Crystal Structure Analysis of FKBP52, Complex with FK506. Determined by X-ray diffraction at 2.01 Å resolution. Released 21 Aug 2013.

Method: X-ray diffraction
Resolution: 2.01 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,060
Mol. weight: 31.8 kDa
Ligands: FK5
Released: 21 Aug 2013

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

Secondary structure: helices and β-sheets

4LAX contains 11 α-helices and 17 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, 17 β-strands

Element	Residues	Length	Sheet
β-strand	23-24	2	1
β-strand	33-39	7	1
β-strand	52-61	10	1
β-strand	66-69	4	1
α-helix	70-72	3
β-strand	77-80	4	1
α-helix	88-94	7
α-helix	97-98	2
β-strand	102-107	6	1
α-helix	109-111	3
β-strand	118	1	2
β-strand	122	1	2
β-strand	128-138	11	1
α-helix	139	1
β-strand	140-141	2	3
β-strand	150-156	7	3
β-strand	169-178	10	3
β-strand	181-191	11	3
α-helix	195-198	4
α-helix	202-208	7
α-helix	211-212	2
β-strand	216-221	6	3
α-helix	223-225	3
β-strand	232	1	4
α-helix	233-235	3
β-strand	237	1	4
β-strand	243-253	11	3
α-helix	254-256	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase FKBP4	A	protein	269	Homo sapiens	Q02790 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4LAX_1 Peptidyl-prolyl cis-trans isomerase FKBP4 (chains A)
MSYYHHHHHHDYDIPTTENLYFQGAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGD
RVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEY
AYGSAGSPPKIPPNATLVFEVELFEFKGEDLTEEEDGGIIRRIQTRGEGYAKPNEGAIVE
VALEGYYKDKLFDQRELRFEIGEGENLDLPYGLERAIQRMEKGEHSIVYLKPSYAFGSVG
KEKFQIPPNAELKYELHLKSFEKAKESWE

Ligands and cofactors

ID	Name	Formula	Copies
FK5	8-deethyl-8-[but-3-enyl]-ascomycin	C44 H69 N O12	1

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

Primary citation

Crystal Structures of the Free and Ligand-Bound FK1-FK2 Domain Segment of FKBP52 Reveal a Flexible Inter-Domain Hinge. Bracher, A., Kozany, C., Hahle, A. et al. J Mol Biol (2013) 425:4134-4144. DOI 10.1016/j.jmb.2013.07.041 · 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
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…
4TW8 3.0 Å, The Fk1-Fk2 domains of FKBP52 in complex with iFit-FL
8FFV 3.01 Å, Cryo-EM structure of the GR-Hsp90-FKBP52 complex

Browse structure collections

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