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1UCH

DEUBIQUITINATING ENZYME UCH-L3 (HUMAN) AT 1.8 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006511biological_processubiquitin-dependent protein catabolic process
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016567biological_processprotein ubiquitination
A0016579biological_processprotein deubiquitination
A0016787molecular_functionhydrolase activity
A0019784molecular_functiondeNEDDylase activity
A0030163biological_processprotein catabolic process
A0043130molecular_functionubiquitin binding
A0043687biological_processpost-translational protein modification
A0101005molecular_functiondeubiquitinase activity
Functional Information from PDB Data
site_idCAT
Number of Residues4
DetailsACTIVE SITE RESIDUES.
ChainResidue
AGLN89
ACYS95
AHIS169
AASP184

Functional Information from PROSITE/UniProt
site_idPS00140
Number of Residues17
DetailsUCH_1 Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site. QtisNACGtigLIHAIA
ChainResidueDetails
AGLN89-ALA105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01393, ECO:0000269|PubMed:19154770, ECO:0000269|PubMed:20380862, ECO:0000269|PubMed:9790970
ChainResidueDetails
ACYS95

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01393
ChainResidueDetails
AHIS169

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU01393
ChainResidueDetails
AGLN89

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for enzyme activity => ECO:0000255|PROSITE-ProRule:PRU01393
ChainResidueDetails
AASP184

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER130

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 9233788, 8639624
ChainResidueDetails
ACYS95
AHIS169
AASP184
AGLN89

site_idMCSA1
Number of Residues4
DetailsM-CSA 597
ChainResidueDetails
AGLN89electrostatic stabiliser
ACYS95covalent catalysis, proton shuttle (general acid/base)
AHIS169proton shuttle (general acid/base)
AASP184electrostatic stabiliser

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PDB entries from 2025-07-02

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