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5FER

Complex of TRIM25 RING with UbcH5-Ub

Functional Information from GO Data
ChainGOidnamespacecontents
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000166molecular_functionnucleotide binding
B0000209biological_processprotein polyubiquitination
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006511biological_processubiquitin-dependent protein catabolic process
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0030514biological_processnegative regulation of BMP signaling pathway
B0031398biological_processpositive regulation of protein ubiquitination
B0032991cellular_componentprotein-containing complex
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0061630molecular_functionubiquitin protein ligase activity
B0061631molecular_functionubiquitin conjugating enzyme activity
B0070936biological_processprotein K48-linked ubiquitination
B1904262biological_processnegative regulation of TORC1 signaling
E0000122biological_processnegative regulation of transcription by RNA polymerase II
E0000166molecular_functionnucleotide binding
E0000209biological_processprotein polyubiquitination
E0004842molecular_functionubiquitin-protein transferase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006511biological_processubiquitin-dependent protein catabolic process
E0016567biological_processprotein ubiquitination
E0016740molecular_functiontransferase activity
E0030514biological_processnegative regulation of BMP signaling pathway
E0031398biological_processpositive regulation of protein ubiquitination
E0032991cellular_componentprotein-containing complex
E0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
E0061630molecular_functionubiquitin protein ligase activity
E0061631molecular_functionubiquitin conjugating enzyme activity
E0070936biological_processprotein K48-linked ubiquitination
E1904262biological_processnegative regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 101
ChainResidue
ACYS13
ACYS16
ALYS21
ACYS33
ACYS36

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 102
ChainResidue
ACYS28
AHIS30
ACYS50
ACYS53

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN D 101
ChainResidue
DCYS28
DHIS30
DCYS50
DCYS53

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN D 102
ChainResidue
DCYS13
DCYS16
DCYS33
DCYS36

site_idAC5
Number of Residues13
Detailsbinding site for Di-peptide GLY F 76 and LYS E 85
ChainResidue
EHIS75
EASN77
EILE78
EILE84
ELEU86
EASP117
EPRO118
ELEU119
EVAL120
EILE123
ETYR134
FARG74
FGLY75

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52

site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CgHnFCgsCL
ChainResidueDetails
ACYS28-LEU37

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues82
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PDB","id":"5EYA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FER","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
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_FI4
Number of Residues150
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"UniProtKB","id":"P62979","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"ADP-ribosylglycine","evidences":[{"source":"UniProtKB","id":"P62979","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues14
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_FI10
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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