1X9D

Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P31723","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P32906","evidenceCode":"ECO:0000250"}]}

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	ARG334
A	ASP463
A	GLU599
A	GLU330

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 19

Chain	Residue	Details
A	GLU330	steric role
A	ARG334	steric role
A	ASP463	electrostatic stabiliser, proton acceptor, proton donor
A	GLU599	increase nucleophilicity, proton acceptor, proton donor

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