1KRF

STRUCTURE OF P. CITRINUM ALPHA 1,2-MANNOSIDASE REVEALS THE BASIS FOR DIFFERENCES IN SPECIFICITY OF THE ER AND GOLGI CLASS I ENZYMES

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004571	molecular_function	mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
A	0005509	molecular_function	calcium ion binding
A	0005975	biological_process	carbohydrate metabolic process
A	0016020	cellular_component	membrane
B	0004571	molecular_function	mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
B	0005509	molecular_function	calcium ion binding
B	0005975	biological_process	carbohydrate metabolic process
B	0016020	cellular_component	membrane

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11714724","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P45700","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11714724","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KKT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KRE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KRF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RI8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RI9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1dl2

Chain	Residue	Details
A	ARG126
A	GLU122
A	GLU409
A	ASP267

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site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1dl2

Chain	Residue	Details
B	ARG126
B	GLU122
B	GLU409
B	ASP267

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