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6J1Y

Semi-open conformation E3 ligase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
B0004842molecular_functionubiquitin-protein transferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL B 1001
ChainResidue
BARG545
BPHE547
BLYS795
BGLU796
BVAL799
BGLU841
BARG845
BGLN848

Functional Information from PROSITE/UniProt
site_idPS01159
Number of Residues26
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. Wekrvdstdrv.YFvnhntktTQWEDP
ChainResidueDetails
ATRP462-PRO487
ATRP502-PRO527

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00104","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Required for ubiquitin-thioester formation","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues33
DetailsDomain: {"description":"WW 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00224","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues33
DetailsDomain: {"description":"WW 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00224","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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