5LDA

Structure of deubiquitinating enzyme homolog (Pyrococcus furiosus JAMM1) in complex with ubiquitin-like SAMP2.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 201

Chain	Residue
A	HIS88
A	HIS90
A	ASP101
B	GLY69

---

site_id	AC2
Number of Residues	4
Details	binding site for residue GOL B 601

Chain	Residue
A	GLU77
B	ILE9
B	LYS42
B	GLU61

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	13
Details	Motif: {"description":"JAMM motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"D4GTS4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28479062","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LD9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"D4GTS4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SAMP2)","evidences":[{"source":"UniProtKB","id":"D4GZE7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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