1KKT

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	ACT_SITE: Proton donor => ECO:0000269|PubMed:11714724

Chain	Residue	Details
A	ASP375
B	ASP375

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P45700

Chain	Residue	Details
A	THR501
B	THR501

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site_id	SWS_FT_FI3
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11714724, ECO:0007744|PDB:1KKT, ECO:0007744|PDB:1KRE, ECO:0007744|PDB:1KRF, ECO:0007744|PDB:2RI8, ECO:0007744|PDB:2RI9

Chain	Residue	Details
A	ASN182
A	ASN366
A	ASN438
B	ASN182
B	ASN366
B	ASN438

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