5JTV

USP7CD-UBL45 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
C	0004843	molecular_function	cysteine-type deubiquitinase activity
C	0016579	biological_process	protein deubiquitination
E	0004843	molecular_function	cysteine-type deubiquitinase activity
E	0016579	biological_process	protein deubiquitination
G	0004843	molecular_function	cysteine-type deubiquitinase activity
G	0016579	biological_process	protein deubiquitination

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

Chain	Residue	Details
A	GLY215-GLN230

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

Chain	Residue	Details
A	TYR448-TYR465

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1228
Details	Domain: {"description":"USP"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25944111","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11923872","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15053880","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16964248","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18716620","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21745816","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22411829","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12507430","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17651432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	300
Details	Domain: {"description":"Ubiquitin-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 789

Chain	Residue	Details
A	ASN218	electrostatic stabiliser
A	CYS223	nucleofuge, nucleophile, proton acceptor, proton donor
A	HIS464	proton acceptor, proton donor
A	ASP481	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 789

Chain	Residue	Details
C	ASN218	electrostatic stabiliser
C	CYS223	nucleofuge, nucleophile, proton acceptor, proton donor
C	HIS464	proton acceptor, proton donor
C	ASP481	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	4
Details	M-CSA 789

Chain	Residue	Details
E	ASN218	electrostatic stabiliser
E	CYS223	nucleofuge, nucleophile, proton acceptor, proton donor
E	HIS464	proton acceptor, proton donor
E	ASP481	electrostatic stabiliser

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site_id	MCSA4
Number of Residues	4
Details	M-CSA 789

Chain	Residue	Details
G	ASN218	electrostatic stabiliser
G	CYS223	nucleofuge, nucleophile, proton acceptor, proton donor
G	HIS464	proton acceptor, proton donor
G	ASP481	electrostatic stabiliser

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