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

2KJH

NMR based structural model of the UBCH8-UBIQUITIN complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000151cellular_componentubiquitin ligase complex
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0019787molecular_functionubiquitin-like protein transferase activity
A0019941biological_processmodification-dependent protein catabolic process
A0031625molecular_functionubiquitin protein ligase binding
A0032020biological_processISG15-protein conjugation
A0032446biological_processprotein modification by small protein conjugation
A0036211biological_processprotein modification process
A0042296molecular_functionISG15 transferase activity
A0043130molecular_functionubiquitin binding
A0045087biological_processinnate immune response
A0061631molecular_functionubiquitin conjugating enzyme activity
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52

site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNVden.GqICLpiI
ChainResidueDetails
ATYR74-ILE89

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
BARG54
BARG72

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Essential for function
ChainResidueDetails
BHIS68

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
BSER65

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
BTHR66

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
BCYS76

site_idSWS_FT_FI6
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
BLYS6

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
BCYS76

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
BLYS11
BLYS48

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
BLYS27

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
ChainResidueDetails
BLYS29

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
BLYS33

site_idSWS_FT_FI12
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
BLYS63

218196

PDB entries from 2024-04-10

PDB statisticsPDBj update infoContact PDBjnumon