Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4AP4

Rnf4 - ubch5a - ubiquitin heterotrimeric complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000151cellular_componentubiquitin ligase complex
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
B0019787molecular_functionubiquitin-like protein transferase activity
B0030514biological_processnegative regulation of BMP signaling pathway
B0031398biological_processpositive regulation of protein ubiquitination
B0031625molecular_functionubiquitin protein ligase binding
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
B1902916biological_processpositive regulation of protein polyubiquitination
B1904262biological_processnegative regulation of TORC1 signaling
E0000122biological_processnegative regulation of transcription by RNA polymerase II
E0000151cellular_componentubiquitin ligase complex
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
E0019787molecular_functionubiquitin-like protein transferase activity
E0030514biological_processnegative regulation of BMP signaling pathway
E0031398biological_processpositive regulation of protein ubiquitination
E0031625molecular_functionubiquitin protein ligase binding
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
E1902916biological_processpositive regulation of protein polyubiquitination
E1904262biological_processnegative regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 800
ChainResidue
ACYS136
ACYS139
ACYS163
ACYS166

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 801
ChainResidue
ACYS158
AHIS160
ACYS177
ACYS180

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 802
ChainResidue
ACYS204
ACYS228
ACYS231
ACYS201

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 803
ChainResidue
ACYS223
AHIS225
ACYS242
ACYS245

Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CgHvFCsqCL
ChainResidueDetails
ACYS158-LEU167
ACYS223-LEU232

site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133
ChainResidueDetails
BLYS85
ELYS85

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20681948, ECO:0007744|PDB:3NG2
ChainResidueDetails
ACYS201
ACYS204
ACYS223
AHIS225
ACYS228
ACYS231
ACYS242
ACYS245

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon