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6DJW

Crystal Structure of pParkin (REP and RING2 deleted)-pUb-UbcH7 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
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
C0006351biological_processDNA-templated transcription
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 A 1001
ChainResidue
ACYS192
ACYS195
ACYS222
ACYS229

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1002
ChainResidue
ACYS177
ACYS180
ACYS246
AHIS249

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1003
ChainResidue
ACYS276
ACYS295
ACYS298
ACYS273

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 1004
ChainResidue
ACYS288
AHIS292
ACYS324
ACYS328

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 1005
ChainResidue
ACYS396
ACYS399
AHIS404
ACYS408

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN A 1006
ChainResidue
ACYS367
ACYS372
ACYS387
ACYS391

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_FI3
Number of Residues1
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"UniProtKB","id":"P62979","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P62979","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues147
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 438
ChainResidueDetails
CLYS86nucleofuge

247536

PDB entries from 2026-01-14

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