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6HUE

ParkinS65N

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0016567biological_processprotein ubiquitination
B0004842molecular_functionubiquitin-protein transferase activity
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0016567biological_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
AGLY361

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN A 506
ChainResidue
AARG348
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

site_idAC9
Number of Residues8
Detailsbinding site for residue SO4 A 509
ChainResidue
AGLN57
AASN58
ALYS161
AARG163
ALYS211
ATHR217
AARG455
AHOH605

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL A 510
ChainResidue
AVAL186
ALEU187
AILE188
APRO189
AGLU207
APHE208

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL A 511
ChainResidue
AHIS227
AVAL250
AGLN252
AARG256
AVAL465
AHOH603

site_idAD3
Number of Residues5
Detailsbinding site for residue CL A 512
ChainResidue
APHE146
ATYR147
ATRP183
ALEU226
AILE229

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BCYS150
BCYS154
BCYS212
BHIS215

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN B 502
ChainResidue
BCYS166
BCYS169
BCYS196
BCYS201

site_idAD6
Number of Residues5
Detailsbinding site for residue ZN B 503
ChainResidue
BCYS238
BTHR240
BCYS241
BCYS260
BCYS263

site_idAD7
Number of Residues4
Detailsbinding site for residue ZN B 504
ChainResidue
BCYS253
BHIS257
BCYS289
BCYS293

site_idAD8
Number of Residues5
Detailsbinding site for residue ZN B 505
ChainResidue
BCYS332
BCYS337
BCYS352
BGLY361
BHOH602

site_idAD9
Number of Residues5
Detailsbinding site for residue ZN B 506
ChainResidue
BARG348
BCYS365
BCYS368
BHIS373
BCYS377

site_idAE1
Number of Residues4
Detailsbinding site for residue ZN B 507
ChainResidue
BCYS418
BCYS421
BCYS436
BCYS441

site_idAE2
Number of Residues4
Detailsbinding site for residue ZN B 508
ChainResidue
BCYS446
BCYS449
BCYS457
BHIS461

site_idAE3
Number of Residues7
Detailsbinding site for residue SO4 B 509
ChainResidue
BHOH603
BASN58
BLYS161
BARG163
BLYS211
BTHR217
BARG455

site_idAE4
Number of Residues6
Detailsbinding site for residue GOL B 510
ChainResidue
BTRP183
BHIS227
BLEU228
BVAL250
BGLN252
BTRP403

site_idAE5
Number of Residues4
Detailsbinding site for residue GOL B 511
ChainResidue
BVAL186
BLEU187
BPRO189
BPHE208

site_idAE6
Number of Residues5
Detailsbinding site for residue CL B 512
ChainResidue
BPHE146
BTYR147
BTRP183
BLEU226
BILE229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues168
DetailsZN_FING: RING-type 0; atypical
ChainResidueDetails
ACYS201-TYR285
BCYS201-TYR285

site_idSWS_FT_FI2
Number of Residues110
DetailsZN_FING: RING-type 1 => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
AILE298-GLU353
BILE298-GLU353

site_idSWS_FT_FI3
Number of Residues128
DetailsZN_FING: IBR-type => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
AHIS373-PRO437
BHIS373-PRO437

site_idSWS_FT_FI4
Number of Residues62
DetailsZN_FING: RING-type 2; atypical => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
AILE298
BILE298
BLEU301
BASN313
BGLN317
BALA320
BCYS323
BLYS349
ALEU301
BGLU353
BHIS433
AASN313
AGLN317
AALA320
ACYS323
ALYS349
AGLU353
AHIS433

site_idSWS_FT_FI7
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23770917
ChainResidueDetails
AARG392
BARG392
BALA397
BLYS412
BARG420
BVAL425
BASN428
BPRO437
AALA397
ALYS412
AARG420
AVAL425
AASN428
APRO437

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25474007
ChainResidueDetails
AASN65
BASN65

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PINK1 => ECO:0000269|PubMed:18957282
ChainResidueDetails
AASN235
BASN235

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:18957282
ChainResidueDetails
APHE277
BPHE277

site_idSWS_FT_FI11
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) => ECO:0000269|PubMed:27534820
ChainResidueDetails
AGLU409
AGLY429
BGLU409
BGLY429

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PDB entries from 2024-07-24

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