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8TQM

Cryo-EM structure of E3 ubiquitin ligase Doa10 from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000837cellular_componentDoa10p ubiquitin ligase complex
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005637cellular_componentnuclear inner membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0030970biological_processretrograde protein transport, ER to cytosol
A0036503biological_processERAD pathway
A0046872molecular_functionmetal ion binding
A0061630molecular_functionubiquitin protein ligase activity
Functional Information from PROSITE/UniProt
site_idPS01159
Number of Residues25
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. Wkfntilltl..YFtkrilesSSYVKP
ChainResidueDetails
ATRP781-PRO805

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues832
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-ALA131
AARG225-LYS468
ALEU513-VAL626
AGLY682-MET739
AGLU798-TYR965
ASER1041-ASN1113
ALYS1190-LYS1213
AGLN1292-SER1319

site_idSWS_FT_FI2
Number of Residues279
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ALEU132-PHE152
ALEU1020-LEU1040
ALEU1114-LEU1134
ALEU1169-LEU1189
AGLN1214-LEU1234
APHE1271-ILE1291
ALEU204-VAL224
ALEU469-ILE489
ALEU492-ILE512
APHE627-PHE647
ALEU661-ILE681
APHE740-PHE760
AILE778-LEU797
AMET966-ILE986

site_idSWS_FT_FI3
Number of Residues179
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
AGLY153-SER203
ASER490-TYR491
ASER648-MET660
AMET761-SER777
ASER987-GLU1019
ATHR1135-SER1168
AARG1235-TYR1270

site_idSWS_FT_FI4
Number of Residues69
DetailsZN_FING: RING-CH-type => ECO:0000255|PROSITE-ProRule:PRU00623
ChainResidueDetails
AASP31-LYS100

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00623
ChainResidueDetails
ACYS39
ACYS42
ACYS56
ACYS58
AHIS66
ACYS69
ACYS90
ACYS93

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

219869

PDB entries from 2024-05-15

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