Phosphopantetheine Adenylytransferase From Escherichia Coli In Complex With 4'-Phosphopantetheine(coaD)

Introduction

Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in the coenzyme A pathway that catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) in the presence of magnesium. Structural details of the catalytic center revealed specific roles for individual amino acid residues involved in substrate binding and catalysis. The side-chain of His18 stabilizes the expected pentacovalent intermediate, whereas the side-chains of Thr10 and Lys42 orient the nucleophile for an in-line displacement mechanism.

Structure Explorer - 1QJC(StructureExplorer1QJC.html)

Experimental Data in PDB summary: PDB summary

Secondary Structure: 2daryStructure

Rasmol Generated Images

Ribbon models: coaD

Space-filled models: coaD2

Ball & stick models: Ballstick

Ligand binding: Rasmol images: bound with PNS; bound with SO4.

CATH Classification

CATHSrch.html

SCOP Classification

SCOPCoaD.html

Structure Alignment

Structurealignment.html

Structurealignment1.html

Structurealignment