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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_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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:26388029
ChainResidueDetails
BCYS90
ECYS90
FARG54
FARG72

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
CHIS68
FHIS68

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:16531995
ChainResidueDetails
CSER65
FSER65

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER67
ESER67

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BGLU507
EGLU507

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
CLYS63
FLYS63

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8BJQ2
ChainResidueDetails
CLYS11
CLYS48
FLYS11
FLYS48

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
CLYS27
FLYS27

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
ChainResidueDetails
CLYS29
FLYS29

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
CLYS33
FLYS33

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PDB entries from 2024-05-01

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