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3BZH

Crystal structure of human ubiquitin-conjugating enzyme E2 E1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000151cellular_componentubiquitin ligase complex
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0019787molecular_functionubiquitin-like protein transferase activity
A0032020biological_processISG15-protein conjugation
A0042296molecular_functionISG15 transferase activity
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070936biological_processprotein K48-linked ubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 200
ChainResidue
ALYS112
AILE130
ALEU135
AHOH215
AHOH258

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHCNInsq.GvICLdiL
ChainResidueDetails
ATYR120-LEU135

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
ACYS131

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER2

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
ChainResidueDetails
ALYS136

224201

PDB entries from 2024-08-28

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