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8S24

Structure of the E3 ubiquitin ligase RNF213, determined by cryoEM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001525biological_processangiogenesis
A0002040biological_processsprouting angiogenesis
A0002376biological_processimmune system process
A0003824molecular_functioncatalytic activity
A0004842molecular_functionubiquitin-protein transferase activity
A0005524molecular_functionATP binding
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0006629biological_processlipid metabolic process
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0019216biological_processregulation of lipid metabolic process
A0042742biological_processdefense response to bacterium
A0046872molecular_functionmetal ion binding
A0051865biological_processprotein autoubiquitination
A0061630molecular_functionubiquitin protein ligase activity
A0070534biological_processprotein K63-linked ubiquitination
A0098792biological_processxenophagy
A0120323biological_processlipid ubiquitination
A0140042biological_processlipid droplet formation
A2000051biological_processnegative regulation of non-canonical Wnt signaling pathway
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues39
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
ACYS3997-LEU4036

site_idSWS_FT_FI2
Number of Residues72
DetailsZN_FING: RZ-type => ECO:0000255|PROSITE-ProRule:PRU01325, ECO:0000269|PubMed:34012115
ChainResidueDetails
AMET4483-THR4555

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Nucleophile; for E3 ubiquitin-lipopolysaccharide ligase activity => ECO:0000255|PROSITE-ProRule:PRU01325
ChainResidueDetails
ACYS4516

site_idSWS_FT_FI4
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:E9Q555
ChainResidueDetails
AGLY1995
AHIS4014
ACYS4017
ACYS4020
ACYS4032
ACYS4035
AGLU2098
AASP2155
AARG2216
ALYS2499
ASER2574
ACYS3997
ACYS4000
ACYS4012

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01325
ChainResidueDetails
ACYS4505
AHIS4509
ACYS4525
ACYS4528

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER208

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER217

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1258

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2273

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
ALYS1151

238268

PDB entries from 2025-07-02

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