2EBN

CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0033925	molecular_function	mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS95

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site_id	ACT
Number of Residues	5
Details

Chain	Residue
A	ASP130
A	GLU132
A	TYR133
A	TYR171
A	TYR173

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Propeptide: {"description":"Removed in mature form","featureId":"PRO_0000011955","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	266
Details	Domain: {"description":"GH18","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01258","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 8535779

Chain	Residue	Details
A	ASP130
A	GLU132

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 926

Chain	Residue	Details
A	ASP130	electrostatic stabiliser
A	GLU132	proton shuttle (general acid/base)

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