1fs5

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1fs5

A DISCOVERY OF THREE ALTERNATE CONFORMATIONS IN THE ACTIVE SITE OF GLUCOSAMINE-6-PHOSPHATE ISOMERASE

Authors Rudino-Pinera, E. Morales-Arrieta, S. Rojas-Trejo, S.P. Horjales, E.
Citation Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase.
Release date 2002-01-04
Exp. Method X-RAY DIFFRACTION
Resolution 1.73 Å
Classification ISOMERASE

Sequence

Chain A (266 residues): Blast Uniprot EC 3.5.99.6
MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYKALVEMHKAGQVSFKHVVTFNMDEYVGLPKE
HPESYYSFMHRNFFDHVDIPAENINLLNGNAPDIDAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIK
TLTHDTRVANSRFFDNDVNQVPKYALTVGVGTLLDAEEVMILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCD
EPSTMELKVKTLRYFNELEAENIKGL
Chain B (266 residues): Blast Uniprot EC 3.5.99.6
MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYKALVEMHKAGQVSFKHVVTFNMDEYVGLPKE
HPESYYSFMHRNFFDHVDIPAENINLLNGNAPDIDAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIK
TLTHDTRVANSRFFDNDVNQVPKYALTVGVGTLLDAEEVMILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCD
EPSTMELKVKTLRYFNELEAENIKGL


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