Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4FJV

Crystal Structure of Human Otubain2 and Ubiquitin Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004843	molecular_function	cysteine-type deubiquitinase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0006508	biological_process	proteolysis
A	0008234	molecular_function	cysteine-type peptidase activity
A	0016579	biological_process	protein deubiquitination
A	0016787	molecular_function	hydrolase activity
A	0035871	biological_process	protein K11-linked deubiquitination
A	0043130	molecular_function	ubiquitin binding
A	0070536	biological_process	protein K63-linked deubiquitination
A	0071108	biological_process	protein K48-linked deubiquitination
A	2000780	biological_process	negative regulation of double-strand break repair
C	0004843	molecular_function	cysteine-type deubiquitinase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0006508	biological_process	proteolysis
C	0008234	molecular_function	cysteine-type peptidase activity
C	0016579	biological_process	protein deubiquitination
C	0016787	molecular_function	hydrolase activity
C	0035871	biological_process	protein K11-linked deubiquitination
C	0043130	molecular_function	ubiquitin binding
C	0070536	biological_process	protein K63-linked deubiquitination
C	0071108	biological_process	protein K48-linked deubiquitination
C	2000780	biological_process	negative regulation of double-strand break repair

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
A	PHE6
A	ASN7
A	SER10
A	LYS44
A	THR45
A	LYS46
A	HOH599
C	ARG20

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	ASP14
C	LYS12
C	ASP14
A	LYS12

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 303

Chain	Residue
A	VAL196
A	TYR220
A	LYS221
A	SER223

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NEH B 101

Chain	Residue
A	GLY49
A	CYS51
A	SER223
B	GLY75

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 301

Chain	Residue
A	ARG20
C	PHE6
C	ASN7
C	SER10
C	THR45
C	GOL303
C	HOH481

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 302

Chain	Residue
A	SER10
A	GLU11
A	HOH581

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 303

Chain	Residue
A	HOH581
C	SER10
C	GOL301

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NEH D 101

Chain	Residue
C	GLY49
C	CYS51
C	SER223
C	HIS224
D	GLY75

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

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

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

Chain	Residue	Details
B	HIS68
D	HIS68

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

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

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: ADP-ribosylglycine => ECO:0000269\|PubMed:28525742

Chain	Residue	Details
B	GLY76
D	GLY76

site_id	SWS_FT_FI6
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

site_id	SWS_FT_FI7
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Chain	Residue	Details
B	GLY76
D	GLY76

site_id	SWS_FT_FI8
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

site_id	SWS_FT_FI9
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

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:16543144, ECO:0000269\|PubMed:25752573, ECO:0000269\|PubMed:25752577, ECO:0000269\|PubMed:34239127

Chain	Residue	Details
B	LYS29
D	LYS29

site_id	SWS_FT_FI11
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

site_id	SWS_FT_FI12
Number of Residues	2
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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)