3EO3

Crystal structure of the N-acetylmannosamine kinase domain of human GNE protein

Summary for 3EO3

• Entry DOI: 10.2210/pdb3eo3/pdb
• Descriptor: Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, ZINC ION, UNKNOWN ATOM OR ION (3 entities in total)
• Functional Keywords: non-protein kinase, sialic acid biosynthesis, structural genomics consortium, sgc, allosteric enzyme, atp-binding, disease mutation, isomerase, kinase, multifunctional enzyme, nucleotide-binding, phosphoprotein, transferase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm : Q9Y223
• Total number of polymer chains: 3
• Total formula weight: 107251.04

Authors

Nedyalkova, L.,Tong, Y.,Rabeh, W.M.,Hong, B.,Tempel, W.,MacKenzie, F.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Weigelt, J.,Bochkarev, A.,Park, H.,Structural Genomics Consortium (SGC) (deposition date: 2008-09-26, release date: 2008-10-07, Last modification date: 2024-02-21)

Primary citation

Tong, Y.,Tempel, W.,Nedyalkova, L.,Mackenzie, F.,Park, H.W.
Crystal structure of the N-acetylmannosamine kinase domain of GNE.
Plos One, 4:e7165-e7165, 2009

PubMed Abstract: UDP-GlcNAc 2-epimerase/ManNAc 6-kinase, GNE, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family.

PubMed: 19841673
DOI: 10.1371/journal.pone.0007165

Experimental method

X-RAY DIFFRACTION (2.84 Å)