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7AY2

Crystal structure of truncated USP1-UAF1 reacted with ubiquitin-prg

Functional Information from GO Data
ChainGOidnamespacecontents
B0004197molecular_functioncysteine-type endopeptidase activity
B0004843molecular_functioncysteine-type deubiquitinase activity
B0006282biological_processregulation of DNA repair
B0016579biological_processprotein deubiquitination
E0004197molecular_functioncysteine-type endopeptidase activity
E0004843molecular_functioncysteine-type deubiquitinase activity
E0006282biological_processregulation of DNA repair
E0016579biological_processprotein deubiquitination
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LISAssDtTVKVWNA
ChainResidueDetails
ALEU90-ALA104
AVAL132-VAL146

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLnnlGNtCYLNSiLQ
ChainResidueDetails
BGLY82-GLN97

site_idPS00973
Number of Residues19
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YgLfAVvmHsGitiss.GHY
ChainResidueDetails
BTYR576-TYR594

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues78
DetailsRepeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues78
DetailsRepeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues78
DetailsRepeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues78
DetailsRepeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues78
DetailsRepeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues78
DetailsRepeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues78
DetailsRepeat: {"description":"WD 8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BH57","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15694335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16531995","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26388029","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
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_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BJQ2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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