5OBK
 
 | | The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-5-(hydroxymethyl)-3-(pyridin-2-ylmethyl)-3,10-diazabicyclo[4.3.1]decan-2-one | | Descriptor: | (1~{S},5~{S},6~{R})-10-[3,5-bis(chloranyl)phenyl]sulfonyl-5-(hydroxymethyl)-3-(pyridin-2-ylmethyl)-3,10-diazabicyclo[4.3.1]decan-2-one, Peptidyl-prolyl cis-trans isomerase FKBP5 | | Authors: | Pomplun, S, Sippel, C, Haehle, A, Bracher, A, Hausch, F. | | Deposit date: | 2017-06-28 | | Release date: | 2018-04-04 | | Last modified: | 2024-01-17 | | Method: | X-RAY DIFFRACTION (1 Å) | | Cite: | Chemogenomic Profiling of Human and Microbial FK506-Binding Proteins.
J. Med. Chem., 61, 2018
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2VN1
 | | Crystal structure of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with FK506 | | Descriptor: | 70 KDA PEPTIDYLPROLYL ISOMERASE, 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN | | Authors: | Kotaka, M, Alag, R, Ye, H, Preiser, P.R, Yoon, H.S, Lescar, J. | | Deposit date: | 2008-01-30 | | Release date: | 2008-05-20 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.35 Å) | | Cite: | Crystal Structure of the Fk506 Binding Domain of Plasmodium Falciparum Fkbp35 in Complex with Fk506.
Biochemistry, 47, 2008
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3EY6
 | | Crystal structure of the FK506-binding domain of human FKBP38 | | Descriptor: | FK506-binding protein 8 | | Authors: | Parthier, C, Maestre-Martinez, M, Neumann, P, Edlich, F, Fischer, G, Luecke, C, Stubbs, M.T. | | Deposit date: | 2008-10-19 | | Release date: | 2009-10-27 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (1.05 Å) | | Cite: | A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding.
J.Mol.Recognit., 24, 2011
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2FKE
 | | FK-506-BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818 | | Descriptor: | 8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN, FK506 BINDING PROTEIN | | Authors: | Becker, J.W, Mckeever, B.M, Rotonda, J. | | Deposit date: | 1993-01-27 | | Release date: | 1994-01-31 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.72 Å) | | Cite: | FK-506-binding protein: three-dimensional structure of the complex with the antagonist L-685,818.
J.Biol.Chem., 268, 1993
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2F2D
 | | Solution structure of the FK506-binding domain of human FKBP38 | | Descriptor: | 38 kDa FK-506 binding protein homolog, FKBP38 | | Authors: | Maestre-Martinez, M, Edlich, F, Jarczowski, F, Weiwad, M, Fischer, G, Luecke, C. | | Deposit date: | 2005-11-16 | | Release date: | 2006-05-02 | | Last modified: | 2024-05-29 | | Method: | SOLUTION NMR | | Cite: | Solution Structure of the FK506-Binding Domain of Human FKBP38
J.BIOMOL.NMR, 34, 2006
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2F4E
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1N1A
 | | Crystal Structure of the N-terminal domain of human FKBP52 | | Descriptor: | FKBP52 | | Authors: | Li, P, Ding, Y, Wu, B, Shu, C, Shen, B, Rao, Z. | | Deposit date: | 2002-10-16 | | Release date: | 2002-12-30 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | Structure of the N-terminal domain of human FKBP52.
Acta Crystallogr.,Sect.D, 59, 2003
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2KFW
 | | Solution structure of full-length SlyD from E.coli | | Descriptor: | FKBP-type peptidyl-prolyl cis-trans isomerase slyD | | Authors: | Martino, L, He, Y, Hands-Taylor, K.L, Valentine, E.R, Kelly, G, Giancola, C, Conte, M.R. | | Deposit date: | 2009-02-28 | | Release date: | 2009-09-15 | | Last modified: | 2024-05-01 | | Method: | SOLUTION NMR | | Cite: | The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity.
Febs J., 276, 2009
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2KE0
 | | Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei | | Descriptor: | Peptidyl-prolyl cis-trans isomerase | | Authors: | Zheng, S, Leeper, T, Napuli, A, Nakazawa, S.H, Varani, G, Seattle Structural Genomics Center for Infectious Disease (SSGCID) | | Deposit date: | 2009-01-21 | | Release date: | 2009-03-03 | | Last modified: | 2024-05-01 | | Method: | SOLUTION NMR | | Cite: | The structure of a Burkholderia pseudomallei immunophilin-inhibitor complex reveals new approaches to antimicrobial development.
Biochem.J., 437, 2011
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4QT3
 | | Crystal structure resolution of Plasmodium falciparum FK506 binding domain (FKBP35) in complex with Rapamycin at 1.4A resolution | | Descriptor: | (2S,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL, FK506-binding protein (FKBP)-type peptidyl-propyl isomerase, RAPAMYCIN IMMUNOSUPPRESSANT DRUG | | Authors: | Bianchin, A, Allemand, F, Bell, A, Chubb, A.J, Guichou, J.-F. | | Deposit date: | 2014-07-07 | | Release date: | 2015-06-10 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (1.4 Å) | | Cite: | Two crystal structures of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with rapamycin at high resolution
Acta Crystallogr.,Sect.D, 71, 2015
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2K8I
 | | Solution structure of E.Coli SlyD | | Descriptor: | Peptidyl-prolyl cis-trans isomerase | | Authors: | Weininger, U, Balbach, J. | | Deposit date: | 2008-09-11 | | Release date: | 2009-03-24 | | Last modified: | 2024-05-01 | | Method: | SOLUTION NMR | | Cite: | NMR solution structure of SlyD from Escherichia coli: spatial separation of prolyl isomerase and chaperone function.
J.Mol.Biol., 387, 2009
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2KI3
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6YF1
 | | FKBP12 in complex with the BMP potentiator compound 8 at 1.12A resolution | | Descriptor: | (1aR,3R,5S,6R,7S,9R,10R,17aS,20S,21R,22S,25R,25aR)-25-Ethyl-10,22-dihydroxy-20-{(1E)-1-[(1R,3R,4R)-4-hydroxy-3-methoxycyclohexyl]prop-1-en-2-yl}-5,7-dimethoxy-1a,3,9,21-tetramethyloctadecahydro-2H-6,10-epoxyoxireno[p]pyrido[2,1-c][1,4]oxazacyclotricosine-11,12,18,24(1aH,14H)-tetrone, Peptidyl-prolyl cis-trans isomerase FKBP1A | | Authors: | Kallen, J. | | Deposit date: | 2020-03-25 | | Release date: | 2021-03-10 | | Last modified: | 2024-01-24 | | Method: | X-RAY DIFFRACTION (1.12 Å) | | Cite: | Phenotypic screen identifies calcineurin-sparing FK506 analogs as BMP potentiators for treatment of acute kidney injury.
Cell Chem Biol, 28, 2021
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6YF2
 | | FKBP12 in complex with the BMP potentiator compound 6 at 1.03A resolution | | Descriptor: | (1~{R},9~{S},12~{S},13~{R},14~{S},17~{R},18~{E},21~{S},23~{S},24~{R},25~{S},27~{R})-23,25-dimethoxy-12-[(~{E})-1-[(1~{R},3~{R},4~{R})-3-methoxy-4-oxidanyl-cyclohexyl]prop-1-en-2-yl]-13,19,21,27-tetramethyl-1,14-bis(oxidanyl)-17-(2-oxidanylidenepropyl)-11,28-dioxa-4-azatricyclo[22.3.1.0^{4,9}]octacos-18-ene-2,3,10,16-tetrone, CADMIUM ION, CHLORIDE ION, ... | | Authors: | Kallen, J. | | Deposit date: | 2020-03-25 | | Release date: | 2021-03-10 | | Last modified: | 2024-01-24 | | Method: | X-RAY DIFFRACTION (1.03 Å) | | Cite: | Phenotypic screen identifies calcineurin-sparing FK506 analogs as BMP potentiators for treatment of acute kidney injury.
Cell Chem Biol, 28, 2021
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6YF0
 | | FKBP12 in complex with the BMP potentiator compound 9 at 1.55 A resolution | | Descriptor: | 18-HYDROXYASCOMYCIN, Peptidyl-prolyl cis-trans isomerase FKBP1A, SULFATE ION | | Authors: | Kallen, J. | | Deposit date: | 2020-03-25 | | Release date: | 2021-03-10 | | Last modified: | 2024-01-24 | | Method: | X-RAY DIFFRACTION (1.55 Å) | | Cite: | Phenotypic screen identifies calcineurin-sparing FK506 analogs as BMP potentiators for treatment of acute kidney injury.
Cell Chem Biol, 28, 2021
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6YF3
 | | FKBP12 in complex with the BMP potentiator compound 10 at 1.00A resolution | | Descriptor: | (1~{R},9~{S},12~{S},13~{R},14~{S},17~{R},18~{E},21~{S},23~{S},24~{R},25~{S},27~{R})-17-ethyl-25-methoxy-12-[(~{E})-1-[(1~{R},3~{R},4~{R})-3-methoxy-4-oxidanyl-cyclohexyl]prop-1-en-2-yl]-13,19,21,27-tetramethyl-1,14,23-tris(oxidanyl)-11,28-dioxa-4-azatricyclo[22.3.1.0^{4,9}]octacos-18-ene-2,3,10,16-tetrone, CADMIUM ION, CHLORIDE ION, ... | | Authors: | Kallen, J. | | Deposit date: | 2020-03-25 | | Release date: | 2021-03-10 | | Last modified: | 2024-01-24 | | Method: | X-RAY DIFFRACTION (1 Å) | | Cite: | Phenotypic screen identifies calcineurin-sparing FK506 analogs as BMP potentiators for treatment of acute kidney injury.
Cell Chem Biol, 28, 2021
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2KR7
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4R0X
 | | Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction | | Descriptor: | Peptidyl-prolyl cis-trans isomerase FKBP5 | | Authors: | LeMaster, D.M, Mustafi, S.M, Brecher, M, Zhang, J, Heroux, A, Li, H.M, Hernandez, G. | | Deposit date: | 2014-08-02 | | Release date: | 2015-05-13 | | Last modified: | 2023-09-20 | | Method: | X-RAY DIFFRACTION (1.2 Å) | | Cite: | Coupling of Conformational Transitions in the N-terminal Domain of the 51-kDa FK506-binding Protein (FKBP51) Near Its Site of Interaction with the Steroid Receptor Proteins.
J.Biol.Chem., 290, 2015
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2KO7
 | | Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with Cycloheximide-N-ethylethanoate | | Descriptor: | Peptidyl-prolyl cis-trans isomerase, ethyl (4-{(2R)-2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl}-2,6-dioxopiperidin-1-yl)acetate | | Authors: | Zheng, S, Leeper, T, Varani, G, Seattle Structural Genomics Center for Infectious Disease (SSGCID) | | Deposit date: | 2009-09-11 | | Release date: | 2009-09-29 | | Last modified: | 2024-05-01 | | Method: | SOLUTION NMR | | Cite: | The structure of a Burkholderia pseudomallei immunophilin-inhibitor complex reveals new approaches to antimicrobial development.
Biochem.J., 437, 2011
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1L1P
 | | Solution Structure of the PPIase Domain from E. coli Trigger Factor | | Descriptor: | trigger factor | | Authors: | Kozlov, G, Trempe, J.-F, Perreault, A, Wong, M, Denisov, A, Ghandi, S, Gehring, K, Ekiel, I, Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) | | Deposit date: | 2002-02-19 | | Release date: | 2003-06-24 | | Last modified: | 2024-05-22 | | Method: | SOLUTION NMR | | Cite: | Solution Structure of the Closed Form of a Peptidyl-Prolyl Isomerase Reveals the Mechanism of Protein Folding
To be Published
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7A6X
 | | Structure of the FKBP51FK1 domain in complex with the macrocyclic SAFit analogue 56 | | Descriptor: | (2S,9S,12R)-2-cyclohexyl-12-[2-(3,4-dimethoxyphenyl)ethyl]-24,27-dimethoxy-11,18,22-trioxa-4-azatetracyclo[21.2.2.113,17.04,9]octacosa-1(25),13(28),14,16,23,26-hexaene-3,10-dione, Peptidyl-prolyl cis-trans isomerase FKBP5 | | Authors: | Bauder, M, Meyners, C, Purder, P, Merz, S, Voll, A, Heymann, T, Hausch, F. | | Deposit date: | 2020-08-27 | | Release date: | 2021-03-17 | | Last modified: | 2024-01-31 | | Method: | X-RAY DIFFRACTION (1.67 Å) | | Cite: | Structure-Based Design of High-Affinity Macrocyclic FKBP51 Inhibitors.
J.Med.Chem., 64, 2021
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7A6W
 | | Structure of the FKBP51FK1 domain in complex with the macrocyclic SAFit analogue 33-(Z) | | Descriptor: | (2S,9S,12R,20Z)-2-cyclohexyl-12-[2-(3,4-dimethoxyphenyl)ethyl]-28,31-dimethoxy-11,18,23,26-tetraoxa-4-azatetracyclo[25.2.2.113,17.04,9]dotriaconta-1(29),13(32),14,16,20,27,30-heptaene-3,10-dione, Peptidyl-prolyl cis-trans isomerase FKBP5 | | Authors: | Bauder, M, Meyners, C, Purder, P, Merz, S, Voll, A, Heymann, T, Hausch, F. | | Deposit date: | 2020-08-27 | | Release date: | 2021-03-17 | | Last modified: | 2024-01-31 | | Method: | X-RAY DIFFRACTION (1.85 Å) | | Cite: | Structure-Based Design of High-Affinity Macrocyclic FKBP51 Inhibitors.
J.Med.Chem., 64, 2021
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4TX0
 | | The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-5-(2-methoxyethoxy)-3-(2-methoxyethyl)-3,10-diazabicyclo[4.3.1]decan-2-one | | Descriptor: | (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-5-(2-methoxyethoxy)-3-(2-methoxyethyl)-3,10-diazabicyclo[4.3.1]decan-2-one, Peptidyl-prolyl cis-trans isomerase FKBP5 | | Authors: | Bischoff, M, Sippel, C, Bracher, A, Hausch, F. | | Deposit date: | 2014-07-02 | | Release date: | 2014-10-15 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (1.03 Å) | | Cite: | Stereoselective Construction of the 5-Hydroxy Diazabicyclo[4.3.1]decane-2-one Scaffold, a Privileged Motif for FK506-Binding Proteins.
Org.Lett., 16, 2014
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4TW6
 | | The Fk1 domain of FKBP51 in complex with iFit1 | | Descriptor: | (3-{(1R)-3-(3,4-dimethoxyphenyl)-1-[({(2S)-1-[(2S)-2-(3,4,5-trimethoxyphenyl)pent-4-enoyl]piperidin-2-yl}carbonyl)oxy]propyl}phenoxy)acetic acid, GLYCEROL, Peptidyl-prolyl cis-trans isomerase FKBP5, ... | | Authors: | Gaali, S, Kirschner, A, Cuboni, S, Hartmann, J, Kozany, C, Balsevich, G, Namendorf, C, Fernandez-Vizarra, P, Almeida, O.F.X, Ruehter, G, Uhr, M, Schmidt, M.V, Touma, C, Bracher, A, Hausch, F. | | Deposit date: | 2014-06-30 | | Release date: | 2014-11-26 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (1.4 Å) | | Cite: | Selective inhibitors of the FK506-binding protein 51 by induced fit.
Nat.Chem.Biol., 11, 2015
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4TW8
 | | The Fk1-Fk2 domains of FKBP52 in complex with iFit-FL | | Descriptor: | 2-(5-{[({3-[(1R)-1-[({(2S)-1-[(2S)-2-[(1S)-cyclohex-2-en-1-yl]-2-(3,4,5-trimethoxyphenyl)acetyl]piperidin-2-yl}carbonyl)oxy]-3-(3,4-dimethoxyphenyl)propyl]phenoxy}acetyl)amino]methyl}-6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid, Peptidyl-prolyl cis-trans isomerase FKBP4 | | Authors: | Gaali, S, Kirschner, A, Cuboni, S, Hartmann, J, Kozany, C, Balsevich, G, Namendorf, C, Fernandez-Vizarra, P, Almeida, O.F.X, Ruehter, G, Uhr, M, Schmidt, M.V, Touma, C, Bracher, A, Hausch, F. | | Deposit date: | 2014-06-30 | | Release date: | 2014-11-26 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (3.003 Å) | | Cite: | Selective inhibitors of the FK506-binding protein 51 by induced fit.
Nat.Chem.Biol., 11, 2015
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