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4BM9

Structure of the autoinhibited Parkin catalytic domain

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 PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1466
ChainResidue
ACYS150
ACYS154
ACYS212
AHIS215

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1467
ChainResidue
ACYS253
AHIS257
ACYS289
ACYS293

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1468
ChainResidue
ACYS449
ACYS457
AHIS461
ACYS446

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1469
ChainResidue
ACYS166
ACYS169
ACYS196
ACYS201

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1470
ChainResidue
ACYS238
ACYS241
ACYS260
ACYS263

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 1471
ChainResidue
ACYS332
ACYS337
ACYS352

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1472
ChainResidue
ACYS365
ACYS368
AHIS373
ACYS377

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1473
ChainResidue
ACYS418
ACYS421
ACYS436
ACYS441

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1474
ChainResidue
AARG163
ALYS211
AARG420
AHOH2045

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1475
ChainResidue
AASN454
AASN454
AARG455
AARG455

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1476
ChainResidue
ALYS151
AHIS302
AARG305
ATYR312
AHOH2087

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1477
ChainResidue
ALYS416
ATRP447
AASN448

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues55
DetailsZinc finger: {"description":"RING-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues31
DetailsZinc finger: {"description":"RING-type 2; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues34
DetailsRegion: {"description":"SYT11 binding 1","evidences":[{"source":"PubMed","id":"12925569","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues36
DetailsRegion: {"description":"SYT11 binding 2","evidences":[{"source":"PubMed","id":"12925569","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23770917","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23770917","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PINK1","evidences":[{"source":"PubMed","id":"18957282","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18957282","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)","evidences":[{"source":"PubMed","id":"27534820","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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