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

8SE9

Cryo-EM structure of a double loaded human UBA7-UBE2L6-ISG15 thioester mimetic complex (Form 2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006974biological_processDNA damage response
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
A0016567biological_processprotein ubiquitination
A0016874molecular_functionligase activity
A0019782molecular_functionISG15 activating enzyme activity
A0019941biological_processmodification-dependent protein catabolic process
A0032020biological_processISG15-protein conjugation
A0032446biological_processprotein modification by small protein conjugation
A0036211biological_processprotein modification process
A0045087biological_processinnate immune response
B0005178molecular_functionintegrin binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0007229biological_processintegrin-mediated signaling pathway
B0009615biological_processresponse to virus
B0009617biological_processresponse to bacterium
B0016567biological_processprotein ubiquitination
B0019941biological_processmodification-dependent protein catabolic process
B0030501biological_processpositive regulation of bone mineralization
B0031386molecular_functionprotein tag activity
B0031397biological_processnegative regulation of protein ubiquitination
B0031625molecular_functionubiquitin protein ligase binding
B0032020biological_processISG15-protein conjugation
B0032461biological_processpositive regulation of protein oligomerization
B0032649biological_processregulation of type II interferon production
B0032728biological_processpositive regulation of interferon-beta production
B0032729biological_processpositive regulation of type II interferon production
B0032733biological_processpositive regulation of interleukin-10 production
B0034340biological_processresponse to type I interferon
B0042742biological_processdefense response to bacterium
B0045071biological_processnegative regulation of viral genome replication
B0045087biological_processinnate immune response
B0045648biological_processpositive regulation of erythrocyte differentiation
B0051607biological_processdefense response to virus
B0060339biological_processnegative regulation of type I interferon-mediated signaling pathway
B0070585biological_processprotein localization to mitochondrion
C0000151cellular_componentubiquitin ligase complex
C0000209biological_processprotein polyubiquitination
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0019787molecular_functionubiquitin-like protein transferase activity
C0019941biological_processmodification-dependent protein catabolic process
C0031625molecular_functionubiquitin protein ligase binding
C0032020biological_processISG15-protein conjugation
C0032446biological_processprotein modification by small protein conjugation
C0036211biological_processprotein modification process
C0042296molecular_functionISG15 transferase activity
C0043130molecular_functionubiquitin binding
C0045087biological_processinnate immune response
C0061631molecular_functionubiquitin conjugating enzyme activity
D0005178molecular_functionintegrin binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0007229biological_processintegrin-mediated signaling pathway
D0009615biological_processresponse to virus
D0009617biological_processresponse to bacterium
D0016567biological_processprotein ubiquitination
D0019941biological_processmodification-dependent protein catabolic process
D0030501biological_processpositive regulation of bone mineralization
D0031386molecular_functionprotein tag activity
D0031397biological_processnegative regulation of protein ubiquitination
D0031625molecular_functionubiquitin protein ligase binding
D0032020biological_processISG15-protein conjugation
D0032461biological_processpositive regulation of protein oligomerization
D0032649biological_processregulation of type II interferon production
D0032728biological_processpositive regulation of interferon-beta production
D0032729biological_processpositive regulation of type II interferon production
D0032733biological_processpositive regulation of interleukin-10 production
D0034340biological_processresponse to type I interferon
D0042742biological_processdefense response to bacterium
D0045071biological_processnegative regulation of viral genome replication
D0045087biological_processinnate immune response
D0045648biological_processpositive regulation of erythrocyte differentiation
D0051607biological_processdefense response to virus
D0060339biological_processnegative regulation of type I interferon-mediated signaling pathway
D0070585biological_processprotein localization to mitochondrion
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNVden.GqICLpiI
ChainResidueDetails
CTYR75-ILE90

site_idPS00865
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PVCTVRyFP
ChainResidueDetails
APRO597-PRO605

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133
ChainResidueDetails
CCYS86
DARG153

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:18606809
ChainResidueDetails
BCYS78
DCYS78

site_idSWS_FT_FI3
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214
ChainResidueDetails
BGLY157
DGLY157

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon