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7US1

Structure of parkin (R0RB) bound to two phospho-ubiquitin molecules

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0016567biological_processprotein ubiquitination
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues55
DetailsZN_FING: RING-type 1 => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS238-CYS293

site_idSWS_FT_FI2
Number of Residues64
DetailsZN_FING: IBR-type => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
AASN313-CYS377

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS238
ACYS241
ACYS253
AHIS257
ACYS260
ACYS263
ACYS289
ACYS293
ACYS332
ACYS337
ACYS352
ACYS360
ACYS365
ACYS368
AHIS373
ACYS377

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PINK1 => ECO:0000250|UniProtKB:O60260
ChainResidueDetails
ATHR175

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O60260
ChainResidueDetails
ATHR217

site_idSWS_FT_FI6
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) => ECO:0000250|UniProtKB:O60260
ChainResidueDetails
ALYS349
ALYS369

219869

PDB entries from 2024-05-15

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