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7R71

Crystal Structure of the UbArk2C-UbcH5b~Ub complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
C0000151cellular_componentubiquitin ligase complex
C0000209biological_processprotein polyubiquitination
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0019787molecular_functionubiquitin-like protein transferase activity
C0031625molecular_functionubiquitin protein ligase binding
C0032991cellular_componentprotein-containing complex
C0036211biological_processprotein modification process
C0051865biological_processprotein autoubiquitination
C0061630molecular_functionubiquitin protein ligase activity
C0061631molecular_functionubiquitin conjugating enzyme activity
C0070062cellular_componentextracellular exosome
C0070936biological_processprotein K48-linked ubiquitination
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
DLYS27-ASP52
ALYS27-ASP52

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
CLYS85
DARG72

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Essential for function
ChainResidueDetails
DHIS68

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
DSER65

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
DTHR66

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
DGLY76

site_idSWS_FT_FI6
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
DLYS6

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
DGLY76

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
DLYS11
DLYS48

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
DLYS27

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
DLYS29

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
DLYS33

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
DLYS63

site_idSWS_FT_FI13
Number of Residues41
DetailsZN_FING: RING-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
ACYS294-ARG335

site_idSWS_FT_FI14
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26656854, ECO:0007744|PDB:5D0I, ECO:0007744|PDB:5D0K, ECO:0007744|PDB:5D0M
ChainResidueDetails
ACYS294
ACYS297
AHIS317
ACYS320

222036

PDB entries from 2024-07-03

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