PDBsum entry 1k7c

Hydrolase

PDB id: 1k7c

Contents

Protein chain

233 a.a. *

Ligands

NAG-NAG-MAN-MAN-MAN-MAN

NAG

SO4 ×4

Waters ×329

* Residue conservation analysis

PDB id:

1k7c

Name:

Hydrolase

Title:

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

Structure:

Rhamnogalacturonan acetylesterase. Chain: a. Engineered: yes

Source:

Aspergillus aculeatus. Organism_taxid: 5053. Expressed in: aspergillus oryzae. Expression_system_taxid: 5062.

Resolution:

1.12Å R-factor: 0.110 R-free: 0.134

Authors:

A.Molgaard,S.Larsen

Key ref:

A.Mølgaard and S.Larsen (2002). A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase. Acta Crystallogr D Biol Crystallogr, 58, 111-119. PubMed id: 11752785

Date:

19-Oct-01 Release date: 28-Dec-01

Protein chain

Q00017  (RHA1_ASPAC) -  Rhamnogalacturonan acetylesterase from Aspergillus aculeatus

Seq: 250 a.a.

Struc: 233 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.1.86 - rhamnogalacturonan acetylesterase.

Acta Crystallogr D Biol Crystallogr 58:111-119 (2002)

PubMed id: 11752785

A branched N-linked glycan at atomic resolution in the 1.12 A structure of rhamnogalacturonan acetylesterase.

A.Mølgaard, S.Larsen.

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.