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5OHK

Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (high resolution)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 601
ChainResidue
ACYS234
ACYS237
ACYS284
ACYS287

site_idAC2
Number of Residues7
Detailsbinding site for residue AYE A 602
ChainResidue
AHIS452
BGLY75
AASN72
AASN75
ACYS77
AGLU159
AGLY451

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLvnlGNtCFMNSlLQ
ChainResidueDetails
AGLY69-GLN84

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. FrLmAVvvHhGdmhs..GHF
ChainResidueDetails
APHE436-PHE453

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18287522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24896179","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25621951","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"24896179","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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