4DRJ: Peptidyl-prolyl cis-trans isomerase FKBP4

o-crystal structure of the PPIase domain of FKBP52, Rapamycin and the FRB fragment of mTOR. Determined by X-ray diffraction at 1.8 Å resolution. Released 6 Feb 2013.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,952
Mol. weight: 28.41 kDa
Ligands: RAP
Released: 6 Feb 2013

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

Secondary structure: helices and β-sheets

4DRJ contains 8 α-helices and 9 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: 2 helices, 9 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
β-strand	77-80	4	1
α-helix	88-94	7
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

Chain B: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	2021-2035	15
α-helix	2036-2040	5
α-helix	2041	1
α-helix	2044-2059	16
α-helix	2065-2091	27
α-helix	2094-2112	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase FKBP4	A	protein	144	Homo sapiens	Q02790 (AlphaFold model)
Serine/threonine-protein kinase mTOR	B	protein	98	Homo sapiens	P42345 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4DRJ_1 Peptidyl-prolyl cis-trans isomerase FKBP4 (chains A)
GAMGMTAEEMKATESGAQSAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVH
YTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSA
GSPPKIPPNATLVFEVELFEFKGE

Sequence of entity 2 (B), FASTA

>4DRJ_2 Serine/threonine-protein kinase mTOR (chains B)
GAMDPEFMEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGR
DLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQ

Ligands and cofactors

ID	Name	Formula	Copies
RAP	Rapamycin immunosuppressant drug	C51 H79 N O13	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Large FK506-Binding Proteins Shape the Pharmacology of Rapamycin. Marz, A.M., Fabian, A.K., Kozany, C. et al. Mol Cell Biol (2013) 33:1357-1367. DOI 10.1128/MCB.00678-12 · 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
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…
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

About this viewer

MolViewer shows 4DRJ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.