4at1

From Proteopedia

Revision as of 13:14, 16 February 2009 by OCA (Talk | contribs)

(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)

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.

Image:4at1.png

Template:STRUCTURE 4at1

STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 2271528

About this Structure

4AT1 is a 4 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Stevens RC, Gouaux JE, Lipscomb WN. Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution. Biochemistry. 1990 Aug 21;29(33):7691-701. PMID:2271528

Page seeded by OCA on Mon Feb 16 15:13:59 2009

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4at1"

Categories: Aspartate carbamoyltransferase | Escherichia coli | Gouaux, J E. | Lipscomb, W N. | Stevens, R C.

4at1

From Proteopedia

STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox