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4LAD

Crystal Structure of the Ube2g2:RING-G2BR complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005783cellular_componentendoplasmic reticulum
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0019787molecular_functionubiquitin-like protein transferase activity
A0032446biological_processprotein modification by small protein conjugation
A0035458biological_processcellular response to interferon-beta
A0036503biological_processERAD pathway
A0042802molecular_functionidentical protein binding
A0051603biological_processproteolysis involved in protein catabolic process
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070936biological_processprotein K48-linked ubiquitination
A1904153biological_processnegative regulation of retrograde protein transport, ER to cytosol
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 701
ChainResidue
BCYS341
BCYS344
BHIS361
BCYS364

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 702
ChainResidue
BCYS356
BHIS358
BCYS375
BCYS378

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OXL B 703
ChainResidue
BASP340

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OXL B 704
ChainResidue
BHOH812

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNIypd.GrVCIsiL
ChainResidueDetails
APHE78-LEU93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
BCYS341-ARG379

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2

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PDB entries from 2024-07-17

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