1azy | pdb_00001azy

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1azy.png

Template:STRUCTURE 1azy

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

Template:ABSTRACT PUBMED 9698549

About this Structure

1AZY is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Feb 16 21:02:22 2009

Proteopedia Page Contributors and Editors (what is this?)

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

1azy | pdb_00001azy

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

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools