1uwl

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1uwl, resolution 1.76Å

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1.76A STRUCTURE OF UROCANATE HYDRATASE FROM PSEUDOMONAS PUTIDA

Overview

Urocanase (EC 4.2.1.49) from Pseudomonas putida was crystallized after, removing one of the seven free thiol groups. The crystal structure was, solved by multiwavelength anomalous diffraction (MAD) using a, seleno-methionine derivative and then refined at 1.14 A resolution. The, enzyme is a symmetric homodimer of 2 x 557 amino acid residues with, tightly bound NAD+ cofactors. Each subunit consists of a typical, NAD-binding domain inserted into a larger core domain that forms the dimer, interface. The core domain has a novel chain fold and accommodates the, substrate urocanate in a surface depression. The NAD domain sits like a, lid on the core domain depression and points with the nicotinamide group, to the substrate. Substrate, nicotinamide and five water molecules are, completely ... [(full description)]

About this Structure

1UWL is a [Single protein] structure of sequence from [Pseudomonas putida] with NAD as [ligand]. Active as [[1]], with EC number [4.2.1.49]. Full crystallographic information is available from [OCA].

Reference

Structure and action of urocanase., Kessler D, Retey J, Schulz GE, J Mol Biol. 2004 Sep 3;342(1):183-94. PMID:15313616

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