1uyp

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spinqualitylabelsall models PDB ID 1uyp Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1uyp, resolution 1.90Å ()
Ligands:	, , ,
Activity:	Beta-fructofuranosidase, with EC number 3.2.1.26
Structural annotation: Resources: InterPro : Ipr013148, Ipr013189, Ipr001362, Ipr008985 Pfam : PF08244, PF00251 SCOP : d1uypa2, d1uypa1, d1uypb1, d1uypb2, d1uypc2, d1uypc1, d1uypd2, d1uypd1, d1uype1, d1uype2, d1uypf1, d1uypf2 UniProt : O33833
Functional annotation: Biological process: metabolic process carbohydrate metabolic process Molecular function: hydrolase activity hydrolase activity, hydrolyzing O-glycosyl compounds beta-fructofuranosidase activity hydrolase activity, acting on glycosyl bonds
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

THE THREE-DIMENSIONAL STRUCTURE OF BETA-FRUCTOSIDASE (INVERTASE) FROM THERMOTOGA MARITIMA

Template:ABSTRACT PUBMED 14973124

About this Structure

1UYP is a 6 chains structure of sequences from Thermotoga maritima. This structure supersedes the now removed PDB entry 1utw. Full crystallographic information is available from OCA.

Reference

• Alberto F, Bignon C, Sulzenbacher G, Henrissat B, Czjzek M. The three-dimensional structure of invertase (beta-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases. J Biol Chem. 2004 Apr 30;279(18):18903-10. Epub 2004 Feb 18. PMID:14973124 doi:10.1074/jbc.M313911200

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