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PDBe Entry: 1q6u 
Crystal structure of FkpA from Escherichia coli
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ISOMERASE
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X-RAY DIFFRACTION
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Resolution: 2.45 Å, R-factor: 21.391%, Free R-factor: 27.663%, Spacegroup: C 2 2 21
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13/01/2004, deposition: 14/08/2003, last revision: 24/02/2009
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Saul, F.A.; Arie, J.-P.; Vulliez-le Normand, B.; Kahn, R.; Betton, J.-M.; Bentley, G.A.
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Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity.
J.MOL.BIOL. vol:335, pag:595-608 (2004) [PubMed ID 14672666 ]
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chaperone, peptidyl-prolyl isomerase, heat shock protein, periplasm, FKBP family
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5.2.1.8 ExPASy BRENDA (A)
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Escherichia coli 562(A)
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FKBP-type peptidyl-prolyl cis-trans isomerase fkpA precursor (EC 5.2.1.8) (PPIase) (Rotamase) P45523 (A)
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A
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1q6h, 1q6i
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| A |
FKBP-type peptidyl-prolyl cis-trans isomerase fkpA |
Protein |
P45523 (FKBA_ECOLI)
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245 |
86% |
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| A |
CESIUM ION |
CS
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