2WE6

Crystal Structure of Plasmodium falciparum Ubiquitin Carboxyl- terminal Hydrolase 3 (UCHL3)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000151	cellular_component	ubiquitin ligase complex
A	0000338	biological_process	protein deneddylation
A	0004843	molecular_function	cysteine-type deubiquitinase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0008234	molecular_function	cysteine-type peptidase activity
A	0016579	biological_process	protein deubiquitination
A	0019784	molecular_function	deNEDDylase activity
A	0043130	molecular_function	ubiquitin binding
B	0000151	cellular_component	ubiquitin ligase complex
B	0000338	biological_process	protein deneddylation
B	0004843	molecular_function	cysteine-type deubiquitinase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0006511	biological_process	ubiquitin-dependent protein catabolic process
B	0008234	molecular_function	cysteine-type peptidase activity
B	0016579	biological_process	protein deubiquitination
B	0019784	molecular_function	deNEDDylase activity
B	0043130	molecular_function	ubiquitin binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:20042598

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000250\|UniProtKB:P09936

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Interaction with ubiquitin => ECO:0000269\|PubMed:20042598

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Important for enzyme activity => ECO:0000250\|UniProtKB:P09936

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1uch

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1uch