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PDBsum entry 4zsc
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PDB id:
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Isomerase
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Title:
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Human cyclophilin d complexed with an inhibitor at room temperature
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Structure:
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Peptidyl-prolyl cis-trans isomerase f, mitochondrial. Chain: a. Fragment: unp residues 44-207. Synonym: ppiase f,cyclophilin d,cypd,cyclophilin f,mitochondrial cyclophilin,cyp-m,rotamase f. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ppif, cyp3. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.50Å
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R-factor:
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0.135
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R-free:
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0.163
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Authors:
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M.Gelin,V.Delfosse,F.Allemand,F.Hoh,Y.Sallaz-Damaz,M.Pirocchi, W.Bourguet,J.-L.Ferrer,G.Labesse,J.-F.Guichou
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Key ref:
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M.Gelin
et al.
(2015).
Combining 'dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography.
Acta Crystallogr D Biol Crystallogr,
71,
1777-1787.
PubMed id:
DOI:
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Date:
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13-May-15
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Release date:
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12-Aug-15
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PROCHECK
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Headers
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References
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P30405
(PPIF_HUMAN) -
Peptidyl-prolyl cis-trans isomerase F, mitochondrial from Homo sapiens
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Seq:
Struc:
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207 a.a.
164 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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DOI no:
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Acta Crystallogr D Biol Crystallogr
71:1777-1787
(2015)
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PubMed id:
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Combining 'dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography.
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M.Gelin,
V.Delfosse,
F.Allemand,
F.Hoh,
Y.Sallaz-Damaz,
M.Pirocchi,
W.Bourguet,
J.L.Ferrer,
G.Labesse,
J.F.Guichou.
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ABSTRACT
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X-ray crystallography is an established technique for ligand screening in
fragment-based drug-design projects, but the required manual handling steps -
soaking crystals with ligand and the subsequent harvesting - are tedious and
limit the throughput of the process. Here, an alternative approach is reported:
crystallization plates are pre-coated with potential binders prior to protein
crystallization and X-ray diffraction is performed directly `in situ' (or
in-plate). Its performance is demonstrated on distinct and relevant therapeutic
targets currently being studied for ligand screening by X-ray crystallography
using either a bending-magnet beamline or a rotating-anode generator. The
possibility of using DMSO stock solutions of the ligands to be coated opens up a
route to screening most chemical libraries.
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