1OTP

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

Summary for 1OTP

Entry DOI	10.2210/pdb1otp/pdb
Descriptor	THYMIDINE PHOSPHORYLASE (1 entity in total)
Functional Keywords	phosphorylase, pyrimidine metabolism, salvage pathway, domain movement, transferase, glycosyltransferase
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	47240.99
Authors	Pugmire, M.J.,Cook, W.J.,Jasanoff, A.,Walter, M.R.,Ealick, S.E. (deposition date: 1997-11-09, release date: 1998-12-09, Last modification date: 2024-02-14)
Primary citation	Pugmire, M.J.,Cook, W.J.,Jasanoff, A.,Walter, M.R.,Ealick, S.E. Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J.Mol.Biol., 281:285-299, 1998 Cited by PubMed: 9698549 DOI: 10.1006/jmbi.1998.1941 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation