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6N13

UbcH7-Ub Complex with R0RBR Parkin and phosphoubiquitin

Functional Information from GO Data
ChainGOidnamespacecontents
B0004842molecular_functionubiquitin-protein transferase activity
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0016567biological_processprotein ubiquitination
C0000151cellular_componentubiquitin ligase complex
C0000166molecular_functionnucleotide binding
C0000209biological_processprotein polyubiquitination
C0003713molecular_functiontranscription coactivator activity
C0003723molecular_functionRNA binding
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006355biological_processregulation of DNA-templated transcription
C0006511biological_processubiquitin-dependent protein catabolic process
C0008283biological_processcell population proliferation
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0019787molecular_functionubiquitin-like protein transferase activity
C0019899molecular_functionenzyme binding
C0031398biological_processpositive regulation of protein ubiquitination
C0031625molecular_functionubiquitin protein ligase binding
C0032446biological_processprotein modification by small protein conjugation
C0036211biological_processprotein modification process
C0044770biological_processcell cycle phase transition
C0045893biological_processpositive regulation of DNA-templated transcription
C0061631molecular_functionubiquitin conjugating enzyme activity
C0070979biological_processprotein K11-linked ubiquitination
C0071383biological_processcellular response to steroid hormone stimulus
C0071385biological_processcellular response to glucocorticoid stimulus
C0097027molecular_functionubiquitin-protein transferase activator activity
C1903955biological_processpositive regulation of protein targeting to mitochondrion
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BCYS253
BHIS257
BCYS289
BCYS293

site_idAC2
Number of Residues3
Detailsbinding site for residue ZN B 502
ChainResidue
BGLU370
BHIS373
BCYS377

site_idAC3
Number of Residues2
Detailsbinding site for residue ZN B 503
ChainResidue
BCYS449
BCYS457

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 504
ChainResidue
BCYS166
BCYS169
BCYS196
BCYS201

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 505
ChainResidue
BCYS238
BCYS241
BCYS260
BCYS263

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN B 506
ChainResidue
BCYS337
BCYS352
BLEU358
BGLY359
BCYS360

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 507
ChainResidue
BCYS418
BARG420
BCYS421
BCYS436

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 508
ChainResidue
BCYS150
BCYS154
BCYS212
BHIS215

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
ALYS27-ASP52
DLYS727-ASP752

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
DARG754
DARG772

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Essential for function
ChainResidueDetails
DHIS768

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
DSER765

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
DTHR766

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
DGLY776
BCYS449
BCYS457
BHIS461
BCYS241
BCYS253
BHIS257
BCYS260
BCYS263
BCYS289
BCYS293
BHIS373

site_idSWS_FT_FI6
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
DLYS706
BCYS436
BCYS441
BCYS446
BCYS337
BCYS352
BCYS360
BCYS365
BCYS368
BCYS377
BCYS418
BCYS421

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
BTHR175
DGLY776

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
DLYS711
DLYS748

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
DLYS727
BLYS369

site_idSWS_FT_FI10
Number of Residues1
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
DLYS729

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
DLYS733

site_idSWS_FT_FI12
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
DLYS763

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 438
ChainResidueDetails
CLYS586nucleofuge

237423

PDB entries from 2025-06-11

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