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Peptidyl-prolyl isomerase ESS1 from Candida albicans
Descriptor:	peptidyl prolyl cis/trans isomerase
Authors:	Li, Z, Li, H, Devasahayam, G, Gemmill, T, Chaturvedi, V, Hanes, S.D, Van Roey, P.
Deposit date:	2005-02-17
Release date:	2005-04-26
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (1.6 Å)
Cite:	The Structure of the Candida albicans Ess1 Prolyl Isomerase Reveals a Well-Ordered Linker that Restricts Domain Mobility Biochemistry, 44, 2005

Crystal Structure of S. cerevisiae Ess1
Descriptor:	Peptidyl-prolyl cis-trans isomerase ESS1
Authors:	Namitz, K.E.W, Alicea-Velazquez, N.L, Cosgrove, M.S, Hanes, S.D.
Deposit date:	2020-10-27
Release date:	2021-03-31
Last modified:	2023-10-18
Method:	X-RAY DIFFRACTION (2.4 Å)
Cite:	Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism. Commun Biol, 4, 2021

PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
Descriptor:	2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, ALANINE, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, ...
Authors:	Noel, J.P, Ranganathan, R, Hunter, T.
Deposit date:	1998-06-21
Release date:	1998-10-14
Last modified:	2023-07-26
Method:	X-RAY DIFFRACTION (1.35 Å)
Cite:	Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell(Cambridge,Mass.), 89, 1997