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PDBe Entry: 1r2t 
CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE
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ISOMERASE
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X-RAY DIFFRACTION
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Resolution: 2.25 Å, R-factor: 18.409%, Free R-factor: 21.999%, Spacegroup: P 21 21 21
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23/12/2003, deposition: 29/09/2003, last revision: 24/02/2009
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Aparicio, R.; Ferreira, S.T.; Polikarpov, I.
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Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.
J.MOL.BIOL. vol:334, pag:1023-1041 (2003) [PubMed ID 14643664 ]
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TIM; Closed loop conformation in the ligand-free state; Conformational heterogeneity; Tim-barrel, ISOMERASE
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5.3.1.1 ExPASy BRENDA (A B)
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Oryctolagus cuniculus(rabbit) 9986(A B)
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Triosephosphate isomerase (EC 5.3.1.1) (TIM) (Triose-phosphate isomerase) P00939 (A B)
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A, B
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1r2r, 1r2s
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| A, B |
Triosephosphate isomerase |
Protein |
P00939 (TPIS_RABIT)
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248 |
99% |
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