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5LD9

Structure of deubiquitinating enzyme homolog, Pyrococcus furiosus JAMM1.

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0046872molecular_functionmetal ion binding
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 201
ChainResidue
AHIS88
AHIS90
AASP101
AHOH360

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 201
ChainResidue
BHIS88
BHIS90
BASP101
BHOH357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:D4GTS4
ChainResidueDetails
AGLU34
BGLU34

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:28479062, ECO:0007744|PDB:5LD9
ChainResidueDetails
AHIS88
AHIS90
AASP101
BHIS88
BHIS90
BASP101

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:D4GTS4
ChainResidueDetails
ASER98
BSER98

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PDB entries from 2024-07-24

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