1K7C

Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution

Summary for 1K7C

• Entry DOI: 10.2210/pdb1k7c/pdb
• Related: 1DEO 1DEX
• Descriptor: rhamnogalacturonan acetylesterase, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: n-linked glycosylation, sgnh-hydrolase, hydrolase
• Biological source: Aspergillus aculeatus
• Total number of polymer chains: 1
• Total formula weight: 26301.31

Authors

Molgaard, A.,Larsen, S. (deposition date: 2001-10-19, release date: 2001-12-28, Last modification date: 2024-10-23)

Primary citation

Molgaard, A.,Larsen, S.
A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase.
Acta Crystallogr.,Sect.D, 58:111-119, 2002

PubMed Abstract: The crystal structure of the glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been refined to a resolution of 1.12 A using synchrotron data collected at 263 K. Both of the two putative N-glycosylation sites at Asn104 and Asn182 are glycosylated and, owing to crystal contacts, the glycan structure at Asn182 is exceptionally well defined in the electron-density maps, showing the six-carbohydrate structure Manalpha1-6(Manalpha1-3)Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAcbeta-Asn182. Equivalent carbohydrate residues were restrained to have similar geometries, but were refined without target values. The refined bond lengths and angles were compared with the values obtained from small-molecule studies that form the basis for the dictionaries used for glycoprotein refinement.

PubMed: 11752785
DOI: 10.1107/S0907444901018479

Experimental method

X-RAY DIFFRACTION (1.12 Å)