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5D1M

Crystal Structure of UbcH5B in Complex with the RING-U5BR Fragment of AO7 (P199A)

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
A0031625molecular_functionubiquitin protein ligase binding
A0032991cellular_componentprotein-containing complex
A0036211biological_processprotein modification process
A0051865biological_processprotein autoubiquitination
A0061630molecular_functionubiquitin protein ligase activity
A0061631molecular_functionubiquitin conjugating enzyme activity
A0070062cellular_componentextracellular exosome
A0070936biological_processprotein K48-linked ubiquitination
B0061630molecular_functionubiquitin protein ligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue OXL A 201
ChainResidue
AGLU140
ATRP141
ALYS144
ATYR145
APEG202

site_idAC2
Number of Residues6
Detailsbinding site for residue PEG A 202
ChainResidue
AOXL201
AHOH397
AARG72
ASER80
ATRP141
ATYR145

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS135
BCYS138
BHIS158
BCYS161

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 302
ChainResidue
BCYS153
BHIS155
BCYS198
BCYS201

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO B 303
ChainResidue
BTHR149
BLYS150
BTHR151
BPRO152
BVAL206
BGLU247
BARG248

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO B 304
ChainResidue
AASN41
AGLN46
AMET147
BLYS150
BTYR154
BARG248

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
ChainResidueDetails
ATYR74-LEU89

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues67
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
BCYS135-ARG202

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:26475854, ECO:0007744|PDB:5D1K, ECO:0007744|PDB:5D1L, ECO:0007744|PDB:5D1M
ChainResidueDetails
BCYS135
BCYS138
BCYS153
BHIS155
BHIS158
BCYS161
BCYS198
BCYS201

221051

PDB entries from 2024-06-12

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