1FCU

CRYSTAL STRUCTURE (TRIGONAL) OF BEE VENOM HYALURONIDASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004415	molecular_function	hyalurononglucosaminidase activity
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0006952	biological_process	defense response
A	0019863	molecular_function	IgE binding
A	0030214	biological_process	hyaluronan catabolic process
A	0044523	biological_process	venom-mediated disruption of extracellular matrix in another organism

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11080624","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"10998264","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1fcq

Chain	Residue	Details
A	ASP111
A	GLU113
A	TYR184
A	TYR227
A	TRP301

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site_id	MCSA1
Number of Residues	5
Details	M-CSA 616

Chain	Residue	Details
A	ASP111	electrostatic stabiliser, modifies pKa, steric role
A	GLU113	activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
A	TYR184	steric role
A	TYR227	electrostatic stabiliser, steric role, transition state stabiliser
A	TRP301	steric role

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