2GFO

Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004843	molecular_function	cysteine-type deubiquitinase activity
A	0016579	biological_process	protein deubiquitination

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1200

Chain	Residue
A	CYS936
A	CYS939
A	CYS985
A	CYS988

---

Functional Information from PROSITE/UniProt

site_id	PS00304
Number of Residues	10
Details	SASP_1 Small, acid-soluble spore proteins, alpha/beta type, signature 1. KgEVAeEFGI

Chain	Residue	Details
A	LYS823-ILE832

---

site_id	PS00972
Number of Residues	16
Details	USP_1 Ubiquitin specific protease (USP) domain signature 1. GLrnlGNtCYMNSiLQ

Chain	Residue	Details
A	GLY778-GLN793

---

site_id	PS00973
Number of Residues	18
Details	USP_2 Ubiquitin specific protease (USP) domain signature 2. YnLfSVsnHyGgldg..GHY

Chain	Residue	Details
A	TYR1051-TYR1068

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q80U87","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP1084
A	CYS786
A	HIS1067
A	ASN781

---