4LAV: Peptidyl-prolyl cis-trans isomerase FKBP4

Name: PDB 4LAV: Crystal Structure Analysis of FKBP52, Crystal Form II
Published: 2013-08-21
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: isomerase

Crystal Structure Analysis of FKBP52, Crystal Form II. Determined by X-ray diffraction at 1.8 Å resolution. Released 21 Aug 2013.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,434
Mol. weight: 55.78 kDa
Released: 21 Aug 2013

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

Secondary structure: helices and β-sheets

4LAV contains 20 α-helices and 36 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
α-helix	17-20	4
β-strand	24	1	1
β-strand	33-39	7	1
α-helix	47-48	2
β-strand	52-61	10	1
β-strand	66-69	4	1
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
β-strand	141	1	3
β-strand	150-156	7	3
β-strand	159	1	4
β-strand	169-178	10	3
β-strand	181-191	11	3
α-helix	195-198	4
α-helix	202-208	7
β-strand	213	1	4
β-strand	216-221	6	3
α-helix	223-225	3
β-strand	232	1	5
α-helix	233-235	3
β-strand	237	1	5
α-helix	238	1
β-strand	243-253	11	3

Chain B: 10 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	17-20	4
β-strand	24	1	6
β-strand	33-39	7	6
β-strand	52-61	10	6
β-strand	66-69	4	6
β-strand	77-80	4	6
α-helix	88-94	7
α-helix	97-98	2
β-strand	102-107	6	6
α-helix	109-111	3
β-strand	128-138	11	6
β-strand	141	1	7
β-strand	150-156	7	7
β-strand	159	1	8
α-helix	164-165	2
β-strand	169-178	10	7
β-strand	181-191	11	7
α-helix	195-198	4
α-helix	202-208	7
β-strand	213	1	8
β-strand	216-221	6	7
α-helix	223-225	3
β-strand	232	1	9
α-helix	233-235	3
β-strand	237	1	9
α-helix	238	1
β-strand	243-253	11	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peptidyl-prolyl cis-trans isomerase FKBP4	A, B	protein	246	Homo sapiens	Q02790 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4LAV_1 Peptidyl-prolyl cis-trans isomerase FKBP4 (chains A, B)
GAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGWLLDGTKFDSSLDRK
DKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSAGSPPKIPPNATLVFEVEL
FEFKGEDLTEEEDGGIIRRIQTRGEGYAKPNEGAIVEVALEGYYKDKLFDQRELRFEIGE
GENLDLPYGLERAIQRMEKGEHSIVYLKPSYAFGSVGKEKFQIPPNAELKYELHLKSFEK
AKESWE

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
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

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