3O65

Crystal structure of a Josephin-ubiquitin complex: Evolutionary restraints on ataxin-3 deubiquitinating activity

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004843	molecular_function	cysteine-type deubiquitinase activity
A	0016579	biological_process	protein deubiquitination
C	0004843	molecular_function	cysteine-type deubiquitinase activity
C	0016579	biological_process	protein deubiquitination
E	0004843	molecular_function	cysteine-type deubiquitinase activity
E	0016579	biological_process	protein deubiquitination
G	0004843	molecular_function	cysteine-type deubiquitinase activity
G	0016579	biological_process	protein deubiquitination

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 192

Chain	Residue
A	LEU156
A	GLN158
A	TYR161

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LYS27-ASP52

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21118805","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3O65","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21118805","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3O65","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"21118805","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3O65","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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