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4S3O

PCGF5-RING1B-UbcH5c complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000151cellular_componentubiquitin ligase complex
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005768cellular_componentendosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006281biological_processDNA repair
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0006915biological_processapoptotic process
A0010008cellular_componentendosome membrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0019787molecular_functionubiquitin-like protein transferase activity
A0030514biological_processnegative regulation of BMP signaling pathway
A0031625molecular_functionubiquitin protein ligase binding
A0036211biological_processprotein modification process
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0051865biological_processprotein autoubiquitination
A0061630molecular_functionubiquitin protein ligase activity
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070062cellular_componentextracellular exosome
A0070936biological_processprotein K48-linked ubiquitination
A0070979biological_processprotein K11-linked ubiquitination
A0085020biological_processprotein K6-linked ubiquitination
A1903955biological_processpositive regulation of protein targeting to mitochondrion
B0000151cellular_componentubiquitin ligase complex
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000151cellular_componentubiquitin ligase complex
D0000209biological_processprotein polyubiquitination
D0004842molecular_functionubiquitin-protein transferase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005768cellular_componentendosome
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006281biological_processDNA repair
D0006511biological_processubiquitin-dependent protein catabolic process
D0006513biological_processprotein monoubiquitination
D0006915biological_processapoptotic process
D0010008cellular_componentendosome membrane
D0016567biological_processprotein ubiquitination
D0016740molecular_functiontransferase activity
D0019787molecular_functionubiquitin-like protein transferase activity
D0030514biological_processnegative regulation of BMP signaling pathway
D0031625molecular_functionubiquitin protein ligase binding
D0036211biological_processprotein modification process
D0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
D0051865biological_processprotein autoubiquitination
D0061630molecular_functionubiquitin protein ligase activity
D0061631molecular_functionubiquitin conjugating enzyme activity
D0070062cellular_componentextracellular exosome
D0070936biological_processprotein K48-linked ubiquitination
D0070979biological_processprotein K11-linked ubiquitination
D0085020biological_processprotein K6-linked ubiquitination
D1903955biological_processpositive regulation of protein targeting to mitochondrion
E0000151cellular_componentubiquitin ligase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 200
ChainResidue
BCYS51
BCYS54
BCYS72
BCYS75

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 201
ChainResidue
BCYS67
BHIS69
BCYS87
BCYS90

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 201
ChainResidue
ECYS54
ECYS72
ECYS75
ECYS51

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 202
ChainResidue
ECYS67
EHIS69
ECYS87
ECYS90

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 201
ChainResidue
CCYS18
CCYS21
CCYS39
CCYS42

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 202
ChainResidue
CCYS34
CHIS36
CCYS53
CCYS56

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 201
ChainResidue
FCYS18
FCYS21
FCYS39
FCYS42

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 202
ChainResidue
FCYS34
FHIS36
FCYS53
FCYS56

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
ChainResidueDetails
ATYR74-LEU89

site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. ClHtFCktCI
ChainResidueDetails
CCYS34-ILE43
BCYS67-ILE76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
BCYS51-ARG91
ECYS51-ARG91

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330
ChainResidueDetails
BSER2
ESER2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:25519132
ChainResidueDetails
BSER41
ESER41

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q9CQJ4
ChainResidueDetails
BLYS112
ELYS112

223166

PDB entries from 2024-07-31

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