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4BVU

Structure of Shigella effector OspG in complex with host UbcH5c- Ubiquitin conjugate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0043657cellular_componenthost cell
A0046777biological_processprotein autophosphorylation
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000166molecular_functionnucleotide binding
B0000209biological_processprotein polyubiquitination
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006281biological_processDNA repair
B0006511biological_processubiquitin-dependent protein catabolic process
B0006513biological_processprotein monoubiquitination
B0006915biological_processapoptotic process
B0006974biological_processDNA damage response
B0010008cellular_componentendosome membrane
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0030514biological_processnegative regulation of BMP signaling pathway
B0036211biological_processprotein modification process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0051865biological_processprotein autoubiquitination
B0061630molecular_functionubiquitin protein ligase activity
B0061631molecular_functionubiquitin conjugating enzyme activity
B0070062cellular_componentextracellular exosome
B0070936biological_processprotein K48-linked ubiquitination
B0070979biological_processprotein K11-linked ubiquitination
B0085020biological_processprotein K6-linked ubiquitination
B1903955biological_processpositive regulation of protein targeting to mitochondrion
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS227-ASP252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues75
DetailsDomain: {"description":"Ubiquitin-like 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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