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	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	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
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	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	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

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	382
Details	Domain: {"description":"OTU","evidences":[{"source":"PROSITE-ProRule","id":"PRU00139","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"15258613","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12704427","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15258613","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Required to orient and stabilize the active site H-224","evidences":[{"source":"PubMed","id":"15258613","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---