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4I1H

Structure of Parkin E3 ligase

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 501
ChainResidue
ACYS150
ACYS154
ACYS212
AHIS215

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS166
ACYS169
ACYS196
ACYS201

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
ACYS241
ACYS260
ACYS263
ACYS238

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 504
ChainResidue
ACYS253
AHIS257
ACYS289
ACYS293

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 505
ChainResidue
ACYS332
ACYS337
ACYS352
ACYS360

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 506
ChainResidue
ACYS365
ACYS368
AHIS373
ACYS377

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 507
ChainResidue
ACYS418
ACYS421
ACYS436
ACYS441

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 508
ChainResidue
ACYS446
ACYS449
ACYS457
AHIS461

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsZN_FING: RING-type 0; atypical
ChainResidueDetails
ASER141-ALA225

site_idSWS_FT_FI2
Number of Residues55
DetailsZN_FING: RING-type 1 => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS238-CYS293

site_idSWS_FT_FI3
Number of Residues64
DetailsZN_FING: IBR-type => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
AASN313-CYS377

site_idSWS_FT_FI4
Number of Residues31
DetailsZN_FING: RING-type 2; atypical => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS418-CYS449

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
ChainResidueDetails
ACYS431

site_idSWS_FT_FI6
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS238
ACYS449
ACYS457
AHIS461
ACYS241
ACYS253
AHIS257
ACYS260
ACYS263
ACYS289
ACYS293
AHIS373

site_idSWS_FT_FI7
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
ChainResidueDetails
ACYS332
ACYS436
ACYS441
ACYS446
ACYS337
ACYS352
ACYS360
ACYS365
ACYS368
ACYS377
ACYS418
ACYS421

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PINK1 => ECO:0000269|PubMed:18957282
ChainResidueDetails
ATHR175

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18957282
ChainResidueDetails
ATHR217

site_idSWS_FT_FI10
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) => ECO:0000269|PubMed:27534820
ChainResidueDetails
ALYS349
ALYS369

223790

PDB entries from 2024-08-14

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