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Ligands
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JZI (2r,4e)-2-[(naphthalen-2-ylcarbonyl)amino]-5-phenylpent-4-enoic acid
Non-standard Residues
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Glycosylation
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Code : 3JYJ   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : Structure-Based Design of Novel PIN1 Inhibitors (II)
Release Data : 2010-04-07
Compound :
mol_id molecule chains synonym
1 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 A,B Rotamase Pin1, PPIase Pin1
ec: 5.2.1.8
fragment: UNP residues 45-163, PIN1 PPIASE DOMAIN
mutation: K77Q, K82Q
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: PIN1
Authors : Greasley, S.E., Ferre, R.A.
Keywords : SBDD, Small Molecule, PPIase, Cell cycle, Isomerase, Nucleus, Phosphoprotein, Rotamase
Exp. method : X-RAY DIFFRACTION ( 1.87 Å )
Citation :

Structure-based design of novel human Pin1 inhibitors (II).

Dong, L.,Marakovits, J.,Hou, X.  et al.
(2010)  Bioorg.Med.Chem.Lett.  20 : 2210 - 2214

PubMed: 20207139
DOI: 10.1016/j.bmcl.2010.02.033

Chain : A, B
UniProt : Q13526 (PIN1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0) 5.2.1.8 PubMed:21497122, PubMed:23623683, PubMed:29686383
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