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4KC9

Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism

Functional Information from GO Data
ChainGOidnamespacecontents
A0000151cellular_componentubiquitin ligase complex
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0008270molecular_functionzinc ion binding
A0015030cellular_componentCajal body
A0016567biological_processprotein ubiquitination
A0016604cellular_componentnuclear body
A0016740molecular_functiontransferase activity
A0019005cellular_componentSCF ubiquitin ligase complex
A0019787molecular_functionubiquitin-like protein transferase activity
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0031463cellular_componentCul3-RING ubiquitin ligase complex
A0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
A0031624molecular_functionubiquitin conjugating enzyme binding
A0031625molecular_functionubiquitin protein ligase binding
A0039585biological_processPKR/eIFalpha signaling
A0046872molecular_functionmetal ion binding
A0061630molecular_functionubiquitin protein ligase activity
A0097413cellular_componentLewy body
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
ACYS344
ACYS347
ACYS362
ACYS367

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 602
ChainResidue
ACYS372
ACYS375
AHIS382
ACYS389

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 603
ChainResidue
ACYS281
ACYS297
ACYS299
ACYS276

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 604
ChainResidue
ACYS304
ACYS307
AHIS312
ACYS317

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 605
ChainResidue
AGLN108
ACYS186
ACYS189
ACYS208
ACYS211

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 606
ChainResidue
ACYS203
AHIS205
ACYS231
ACYS236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15236971","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24058416","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WD2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2M9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23707686","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24058416","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2M9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KC9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Z1K5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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