3C0R

Structure of Ovarian Tumor (OTU) domain in complex with Ubiquitin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004843	molecular_function	cysteine-type deubiquitinase activity
A	0016579	biological_process	protein deubiquitination
A	0030433	biological_process	ubiquitin-dependent ERAD pathway
A	0101005	molecular_function	deubiquitinase activity
C	0004843	molecular_function	cysteine-type deubiquitinase activity
C	0016579	biological_process	protein deubiquitination
C	0030433	biological_process	ubiquitin-dependent ERAD pathway
C	0101005	molecular_function	deubiquitinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 3CN B 76

Chain	Residue
A	ASP116
A	ASP117
A	CYS120
A	TRP175
A	ILE221
A	HIS222
B	GLY75

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE 3CN D 76

Chain	Residue
C	CYS120
C	TRP175
C	ILE221
C	HIS222
D	GLY75
C	ASP116
C	ASP117

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Functional Information from PROSITE/UniProt

site_id	PS00028
Number of Residues	23
Details	ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cnt..CqmtFvgerevarHaestgH

Chain	Residue	Details
A	CYS272-HIS294

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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	SITE: Interacts with activating enzyme

Chain	Residue	Details
B	ARG54
B	ARG72
D	ARG54
D	ARG72

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Essential for function

Chain	Residue	Details
B	HIS68
D	HIS68
C	ASP117
C	HIS294

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291

Chain	Residue	Details
B	SER65
D	SER65

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457

Chain	Residue	Details
B	THR66
D	THR66

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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
A	LYS160
B	LYS63
C	LYS160
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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