2EKE

Structure of a SUMO-binding-motif mimic bound to Smt3p-Ubc9p: conservation of a noncovalent Ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000022	biological_process	mitotic spindle elongation
A	0000166	molecular_function	nucleotide binding
A	0000794	cellular_component	condensed nuclear chromosome
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005694	cellular_component	chromosome
A	0016740	molecular_function	transferase activity
A	0016925	biological_process	protein sumoylation
A	0019789	molecular_function	SUMO transferase activity
A	0051301	biological_process	cell division
A	0061656	molecular_function	SUMO conjugating enzyme activity
B	0000022	biological_process	mitotic spindle elongation
B	0000166	molecular_function	nucleotide binding
B	0000794	cellular_component	condensed nuclear chromosome
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005694	cellular_component	chromosome
B	0016740	molecular_function	transferase activity
B	0016925	biological_process	protein sumoylation
B	0019789	molecular_function	SUMO transferase activity
B	0051301	biological_process	cell division
B	0061656	molecular_function	SUMO conjugating enzyme activity

Functional Information from PROSITE/UniProt

site_id	PS00183
Number of Residues	16
Details	UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNVyps.GtICLsiL

Chain	Residue	Details
A	TYR82-LEU97

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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