2bes

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2bes

STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE, RPIB, RV2465C, IN COMPLEX WITH 4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID.

Authors Roos, A.K. Burgos, E. Ericsson, D.J. Salmon, L. Mowbray, S.L.
Citation Competitive inhibitors of Mycobacterium tuberculosis ribose-5-phosphate isomerase B reveal new information about the reaction mechanism.
Release date 2005-02-23
Exp. Method X-RAY DIFFRACTION
Resolution 2.1 Å
Classification ISOMERASE

Sequence

Chain A (172 residues): Blast Uniprot
MAHHHHHHSGMSGMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIAAATRTVADPGSLGIVLGG
SGNGEQIAANKVPGARCALAWSVQTAALAREHNNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYER
THEAPPVPGAPA
Chain B (172 residues): Blast Uniprot
MAHHHHHHSGMSGMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIAAATRTVADPGSLGIVLGG
SGNGEQIAANKVPGARCALAWSVQTAALAREHNNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYER
THEAPPVPGAPA
Chain C (172 residues): Blast Uniprot
MAHHHHHHSGMSGMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIAAATRTVADPGSLGIVLGG
SGNGEQIAANKVPGARCALAWSVQTAALAREHNNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYER
THEAPPVPGAPA
Chain D (172 residues): Blast Uniprot
MAHHHHHHSGMSGMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIAAATRTVADPGSLGIVLGG
SGNGEQIAANKVPGARCALAWSVQTAALAREHNNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYER
THEAPPVPGAPA
Chain E (172 residues): Blast Uniprot
MAHHHHHHSGMSGMRVYLGADHAGYELKQRIIEHLKQTGHEPIDCGALRYDADDDYPAFCIAAATRTVADPGSLGIVLGG
SGNGEQIAANKVPGARCALAWSVQTAALAREHNNAQLIGIGGRMHTVAEALAIVDAFVTTPWSKAQRHQRRIDILAEYER
THEAPPVPGAPA


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