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5CAW

Structure of Pediculus humanus Parkin bound to phospho-ubiquitin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0016567biological_processprotein ubiquitination
C0004842molecular_functionubiquitin-protein transferase activity
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0008270molecular_functionzinc ion binding
C0016567biological_processprotein ubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
ACYS151
ACYS155
ACYS213
AHIS216

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1002
ChainResidue
ACYS167
ACYS170
ACYS197
ACYS202

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1003
ChainResidue
ACYS243
ACYS262
ACYS265
ACYS240

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 1004
ChainResidue
ACYS255
AHIS259
ACYS291
ACYS295

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 1005
ChainResidue
ACYS334
ACYS339
ACYS354
ACYS356

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN A 1006
ChainResidue
ACYS361
ACYS364
AHIS369
ACYS373

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN A 1007
ChainResidue
ACYS415
ACYS418
ACYS433
ACYS438

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN A 1008
ChainResidue
ACYS443
ACYS446
ACYS454
AHIS458

site_idAC9
Number of Residues4
Detailsbinding site for residue SO4 A 1009
ChainResidue
ASER183
ATRP184
AARG258
AHOH1104

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN C 1001
ChainResidue
CCYS151
CCYS155
CCYS213
CHIS216

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN C 1002
ChainResidue
CCYS167
CCYS170
CCYS197
CCYS202

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN C 1003
ChainResidue
CCYS240
CCYS243
CCYS262
CCYS265

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN C 1004
ChainResidue
CCYS255
CHIS259
CCYS291
CCYS295

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN C 1005
ChainResidue
CCYS334
CCYS339
CCYS354
CCYS356

site_idAD6
Number of Residues4
Detailsbinding site for residue ZN C 1006
ChainResidue
CCYS361
CCYS364
CHIS369
CCYS373

site_idAD7
Number of Residues4
Detailsbinding site for residue ZN C 1007
ChainResidue
CCYS415
CCYS418
CCYS433
CCYS438

site_idAD8
Number of Residues4
Detailsbinding site for residue ZN C 1008
ChainResidue
CCYS443
CCYS446
CCYS454
CHIS458

site_idAD9
Number of Residues3
Detailsbinding site for residue SO4 C 1009
ChainResidue
CTRP184
CLYS232
CARG258

site_idAE1
Number of Residues8
Detailsbinding site for residue SO4 C 1010
ChainResidue
AHIS441
APRO449
CGLY195
CVAL196
CCYS197
CCYS202
CGLU203
CGLY204

site_idAE2
Number of Residues2
Detailsbinding site for residue SO4 C 1011
ChainResidue
CTHR310
CASP311

site_idAE3
Number of Residues3
Detailsbinding site for residue SO4 D 101
ChainResidue
DARG42
DARG72
DARG74

site_idAE4
Number of Residues4
Detailsbinding site for Di-peptide GLY D 75 and 3CN D 76
ChainResidue
CASP346
CCYS349
CARG351
DARG74

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 Residues4
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
BARG54
BARG72
DARG54
DARG72

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Essential for function
ChainResidueDetails
BHIS68
DHIS68

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
BSEP65
DSEP65

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
BTHR66
DTHR66

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
B3CN76
D3CN76

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
BLYS6
DLYS6

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
ACYS151
ACYS446
ACYS454
AHIS458
CCYS151
CCYS155
CCYS167
CCYS170
CCYS197
CCYS202
CCYS213
B3CN76
CHIS216
CCYS443
CCYS446
CCYS454
CHIS458
ACYS167
D3CN76
ACYS197
ACYS202
ACYS213
AHIS216
ACYS443

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
BLYS11
ACYS339
ACYS354
ACYS356
ACYS361
ACYS364
AHIS369
ACYS373
ACYS415
ACYS418
ACYS433
BLYS48
ACYS438
CCYS240
CCYS243
CCYS255
CHIS259
CCYS262
CCYS265
CCYS291
CCYS295
CCYS334
DLYS11
CCYS339
CCYS354
CCYS356
CCYS361
CCYS364
CHIS369
CCYS373
CCYS415
CCYS418
CCYS433
DLYS48
CCYS438
ACYS262
ACYS265
ACYS291
ACYS295
ACYS334

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
BLYS27
DLYS27
ATYR314
CHIS304
CARG307
CTYR314

site_idSWS_FT_FI10
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
BLYS29
DLYS29

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
BLYS33
DLYS33

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
BLYS63
DLYS63

218853

PDB entries from 2024-04-24

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