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PDBsum entry 5i98
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PDB id:
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Isomerase
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Title:
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Structure of apo fkbp12(p104g) from c. Albicans
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Structure:
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Fk506-binding protein 1. Chain: a, b. Synonym: fkbp,peptidyl-prolyl cis-trans isomerase,ppiase,rapamycin- binding protein. Engineered: yes. Mutation: yes
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Source:
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Candida albicans (strain sc5314 / atcc mya- 2876). Yeast. Organism_taxid: 237561. Strain: sc5314 / atcc mya-2876. Gene: rbp1, rbp11, cao19.11186, cao19.3702, rbp2, rbp12, caj7.0299, cao19.13810, cao19.6452. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.00Å
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R-factor:
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0.182
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R-free:
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0.195
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Authors:
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M.A.Schumacher
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Key ref:
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N.K.Tonthat
et al.
(2016).
Structures of Pathogenic Fungal FKBP12s Reveal Possible Self-Catalysis Function.
Mbio,
7,
e00492.
PubMed id:
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Date:
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19-Feb-16
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Release date:
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14-Sep-16
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PROCHECK
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Headers
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References
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P28870
(FKBP_CANAL) -
FK506-binding protein 1 from Candida albicans (strain SC5314 / ATCC MYA-2876)
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Seq:
Struc:
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124 a.a.
120 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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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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Mbio
7:e00492
(2016)
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PubMed id:
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Structures of Pathogenic Fungal FKBP12s Reveal Possible Self-Catalysis Function.
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N.K.Tonthat,
P.R.Juvvadi,
H.Zhang,
S.C.Lee,
R.Venters,
L.Spicer,
W.J.Steinbach,
J.Heitman,
M.A.Schumacher.
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ABSTRACT
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Links
