Literature summary for 3.2.1.209 extracted from

Vallee, F.; Lipari, F.; Yip, P.; Sleno, B.; Herscovics, A.; Howell, P.L.
Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control (2000), EMBO J., 19, 581-588 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Pichia pastoris as secreted glycoprotein, beginning at residue 34	Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure reaveals a (alphaalpha)7-barrel in which an N?glycan from one molecule extends into the barrel of an adjacent molecule, interacting with the essential acidic residues and calcium ion	Saccharomyces cerevisiae

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	-	Saccharomyces cerevisiae	5783	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	the calcium ion binds to the carbonyl oxygen and the Ogamma of residue T525, and to four water molecules that are in turn hydrogen-bonded to one of the two carboxylate groups of residues E279, E435, E438 and E503	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P32906	-	-
Saccharomyces cerevisiae ATCC 204508	P32906	-	-

Synonyms

Synonyms	Comment	Organism
MNS1	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)