1otp

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File:1otp.png

Template:STRUCTURE 1otp

STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASESTRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE

Template:ABSTRACT PUBMED 9698549

About this StructureAbout this Structure

1OTP is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Pugmire MJ, Cook WJ, Jasanoff A, Walter MR, Ealick SE. Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J Mol Biol. 1998 Aug 14;281(2):285-99. PMID:9698549 doi:10.1006/jmbi.1998.1941

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OCA

[1] Pugmire MJ, Cook WJ, Jasanoff A, Walter MR, Ealick SE. Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J Mol Biol. 1998 Aug 14;281(2):285-99. PMID:9698549 doi:10.1006/jmbi.1998.1941

[xtra 1]