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1CMX

STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0006511biological_processubiquitin-dependent protein catabolic process
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0010992biological_processubiquitin recycling
A0016787molecular_functionhydrolase activity
A0030163biological_processprotein catabolic process
A0051604biological_processprotein maturation
C0004843molecular_functioncysteine-type deubiquitinase activity
C0005737cellular_componentcytoplasm
C0006508biological_processproteolysis
C0006511biological_processubiquitin-dependent protein catabolic process
C0008233molecular_functionpeptidase activity
C0008234molecular_functioncysteine-type peptidase activity
C0010992biological_processubiquitin recycling
C0016787molecular_functionhydrolase activity
C0030163biological_processprotein catabolic process
C0051604biological_processprotein maturation
Functional Information from PDB Data
site_idCAT
Number of Residues6
DetailsCYSTEINE PROTEASE
ChainResidue
ACYS90
AHIS166
AASP181
CCYS490
CHIS566
CASP581

Functional Information from PROSITE/UniProt
site_idPS00140
Number of Residues17
DetailsUCH_1 Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site. QsvkNACGlyaILHSLS
ChainResidueDetails
AGLN84-SER100

site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS327-ASP352

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsRegion: {"description":"Interaction with ubiquitin"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10091","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Important for enzyme activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 10406793, 8639624
ChainResidueDetails
AASP181
ACYS90
ACYS90
AHIS166
AGLN84

site_idCSA2
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 10406793, 8639624
ChainResidueDetails
CHIS566
CCYS490
CCYS490
CGLN484
CASP581

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PDB entries from 2025-12-10

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