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PDBsum entry 8ccb
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PDB id:
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Isomerase
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Title:
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The fk1 domain of fkbp51 in complex with 2-(3-((1r)-1-(((2s)-1-(2-(5- chlorothiophen-2-yl)-2-cyclohexylacetyl)piperidine-2-carbonyl)oxy)-3- (3,4-dimethoxyphenyl)propyl)phenoxy)acetic acid
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Structure:
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Peptidyl-prolyl cis-trans isomerase fkbp5. Chain: a. Synonym: ppiase fkbp5,51 kda fk506-binding protein,fkbp-51,54 kda progesterone receptor-associated immunophilin,androgen-regulated protein 6,ff1 antigen,fk506-binding protein 5,fkbp-5,fkbp54,p54, hsp90-binding immunophilin,rotamase. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: fkbp5, aig6, fkbp51. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
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Resolution:
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1.70Å
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R-factor:
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0.209
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R-free:
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0.236
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Authors:
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C.Meyners,F.H.Knaup,C.M.Walz,F.Hausch
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Key ref:
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F.H.Knaup
et al.
Structure-Based discovery of a new selectivity-Enabli motif for the fk506-Binding protein 51..
J med chem,
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PubMed id:
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Date:
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27-Jan-23
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Release date:
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26-Apr-23
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PROCHECK
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Headers
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References
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Q13451
(FKBP5_HUMAN) -
Peptidyl-prolyl cis-trans isomerase FKBP5 from Homo sapiens
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Seq:
Struc:
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457 a.a.
128 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 6 residue positions (black
crosses)
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Enzyme class:
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E.C.5.2.1.8
- peptidylprolyl isomerase.
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Reaction:
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[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
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Peptidylproline (omega=180)
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=
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peptidylproline (omega=0)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Links
