2FUQ

Crystal Structure of Heparinase II

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008201	molecular_function	heparin binding
A	0015021	molecular_function	heparin-sulfate lyase activity
A	0016829	molecular_function	lyase activity
A	0030211	biological_process	heparin proteoglycan catabolic process
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0047488	molecular_function	heparin lyase activity
B	0008201	molecular_function	heparin binding
B	0015021	molecular_function	heparin-sulfate lyase activity
B	0016829	molecular_function	lyase activity
B	0030211	biological_process	heparin proteoglycan catabolic process
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0047488	molecular_function	heparin lyase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"20404324","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20404324","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16565082","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20404324","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"16565082","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20404324","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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