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3F92

Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington Interacting Protein 2) M172A mutant crystallized at pH 8.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
A0010994biological_processfree ubiquitin chain polymerization
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0019787molecular_functionubiquitin-like protein transferase activity
A0031625molecular_functionubiquitin protein ligase binding
A0032433cellular_componentfilopodium tip
A0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
A0032446biological_processprotein modification by small protein conjugation
A0034450molecular_functionubiquitin-ubiquitin ligase activity
A0035458biological_processcellular response to interferon-beta
A0060340biological_processpositive regulation of type I interferon-mediated signaling pathway
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070936biological_processprotein K48-linked ubiquitination
A1903265biological_processpositive regulation of tumor necrosis factor-mediated signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 A 201
ChainResidue
ASER185
ALYS186
ATHR192

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PG4 A 202
ChainResidue
AVAL151
AARG176

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 203
ChainResidue
ACYS92
ALYS97
AASP124
APRO125

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TRS A 204
ChainResidue
AASP30
ALEU31
AGLY173

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 205
ChainResidue
AASP0
AGLU20
AGLN99
AHOH216
AHOH265

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues17
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. WHPNIssvtGaICLdiL
ChainResidueDetails
ATRP80-LEU96

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
ACYS92

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.11, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS14

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER159

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS14

226707

PDB entries from 2024-10-30

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