3M63

Crystal structure of Ufd2 in complex with the ubiquitin-like (UBL) domain of Dsk2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000151	cellular_component	ubiquitin ligase complex
A	0000209	biological_process	protein polyubiquitination
A	0004842	molecular_function	ubiquitin-protein transferase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0016567	biological_process	protein ubiquitination
A	0016740	molecular_function	transferase activity
A	0031398	biological_process	positive regulation of protein ubiquitination
A	0034450	molecular_function	ubiquitin-ubiquitin ligase activity
A	0036503	biological_process	ERAD pathway
A	0061630	molecular_function	ubiquitin protein ligase activity
A	0070936	biological_process	protein K48-linked ubiquitination
A	0071361	biological_process	cellular response to ethanol

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 1PE A 962

Chain	Residue
A	ILE329
A	PRO491
A	PHE492
A	GLN494
A	GLU560
A	K963
A	HOH1138

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K A 963

Chain	Residue
A	HOH1138
A	PRO491
A	1PE962

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Functional Information from PROSITE/UniProt

site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KeaInKangIPvanQrLIYsGkilkD

Chain	Residue	Details
B	LYS28-ASP53

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	74
Details	Domain: {"description":"U-box"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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