2apc

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Revision as of 15:35, 25 July 2012

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spinqualitylabelsall models PDB ID 2apc Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
2apc, resolution 1.50Å ()
Ligands:	, ,
Activity:	Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, with EC number 2.4.1.101
Related:	1foa, 1fo9, 1fo8
Structural annotation: Resources: CATH : 2Apca01, 2Apca02 InterPro : Ipr004139 Pfam : PF03071 UniProt : P27115
Functional annotation: Cellular component: Golgi apparatus Golgi membrane membrane integral to membrane Biological process: protein amino acid N-linked glycosylation Molecular function: alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity transferase activity transferase activity, transferring glycosyl groups
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP-GlcNAc phosphonate 2 About this Structure 3 See Also 4 Reference

Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP-GlcNAc phosphonate

Template:ABSTRACT PUBMED 16769084

About this Structure

2apc is a 1 chain structure of O-GlcNAc transferase with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

See Also

• O-GlcNAc transferase

Reference

• Gordon RD, Sivarajah P, Satkunarajah M, Ma D, Tarling CA, Vizitiu D, Withers SG, Rini JM. X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues. J Mol Biol. 2006 Jun 30;360(1):67-79. Epub 2006 May 12. PMID:16769084 doi:http://dx.doi.org/10.1016/j.jmb.2006.04.058