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4JQU

Crystal structure of Ubc7p in complex with the U7BR of Cue1p

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000209biological_processprotein polyubiquitination
A0000837cellular_componentDoa10p ubiquitin ligase complex
A0000839cellular_componentHrd1p ubiquitin ligase ERAD-L complex
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006325biological_processchromatin organization
A0006511biological_processubiquitin-dependent protein catabolic process
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0031505biological_processfungal-type cell wall organization
A0036503biological_processERAD pathway
A0046686biological_processresponse to cadmium ion
A0061631molecular_functionubiquitin conjugating enzyme activity
A1990389cellular_componentCUE1-UBC7 ubiquitin-conjugating enzyme complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTB A 301
ChainResidue
ALYS29
AASP38
AHOH481
AHOH497
BLYS154
BPHE155
BHIS156
BGLU174
BLYS177

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 302
ChainResidue
AGLY23
AILE24
AHOH492
AHOH493
BLEU180

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 303
ChainResidue
ASER76
AILE77
ALEU78
AASN137
AHOH476

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. LHPNIypn.GeVCIsiL
ChainResidueDetails
ALEU78-LEU93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388
ChainResidueDetails
ACYS89

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:17310239
ChainResidueDetails
ACYS89

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PDB entries from 2025-06-18

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