2WDT

Crystal structure of Plasmodium falciparum UCHL3 in complex with the suicide inhibitor UbVME

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	0008233	molecular_function	peptidase activity
A	0008234	molecular_function	cysteine-type peptidase activity
A	0016579	biological_process	protein deubiquitination
A	0016787	molecular_function	hydrolase activity
A	0019784	molecular_function	deNEDDylase activity
A	0043130	molecular_function	ubiquitin binding
C	0000151	cellular_component	ubiquitin ligase complex
C	0000338	biological_process	protein deneddylation
C	0004843	molecular_function	cysteine-type deubiquitinase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0008233	molecular_function	peptidase activity
C	0008234	molecular_function	cysteine-type peptidase activity
C	0016579	biological_process	protein deubiquitination
C	0016787	molecular_function	hydrolase activity
C	0019784	molecular_function	deNEDDylase activity
C	0043130	molecular_function	ubiquitin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL D 1076

Chain	Residue
D	ARG42

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site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 1076

Chain	Residue
B	ARG42

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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	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:20042598

Chain	Residue	Details
A	CYS92
C	CYS92
D	ARG54
D	ARG72

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

Chain	Residue	Details
A	HIS164
C	HIS164

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

Chain	Residue	Details
A	ASP33
A	ASP157
A	SER219
C	ASP33
C	ASP157
C	SER219

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

Chain	Residue	Details
A	ASP179
C	ASP179

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site_id	SWS_FT_FI5
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603

Chain	Residue	Details
B	LYS6
D	LYS6

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site_id	SWS_FT_FI6
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106

Chain	Residue	Details
B	LYS63
D	LYS63

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site_id	SWS_FT_FI7
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144

Chain	Residue	Details
B	LYS11
B	LYS48
D	LYS11
D	LYS48

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site_id	SWS_FT_FI8
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860

Chain	Residue	Details
B	LYS27
D	LYS27

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site_id	SWS_FT_FI9
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127

Chain	Residue	Details
B	LYS29
D	LYS29

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site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577

Chain	Residue	Details
B	LYS33
D	LYS33

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