Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7OD1

Crystal structure of RBR ubiquitin ligase ARIH2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000151cellular_componentubiquitin ligase complex
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006511biological_processubiquitin-dependent protein catabolic process
A0008270molecular_functionzinc ion binding
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0031466cellular_componentCul5-RING ubiquitin ligase complex
A0031624molecular_functionubiquitin conjugating enzyme binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0046872molecular_functionmetal ion binding
A0048588biological_processdevelopmental cell growth
A0061630molecular_functionubiquitin protein ligase activity
A0070534biological_processprotein K63-linked ubiquitination
A0070936biological_processprotein K48-linked ubiquitination
A0071425biological_processhematopoietic stem cell proliferation
A1903955biological_processpositive regulation of protein targeting to mitochondrion
B0000151cellular_componentubiquitin ligase complex
B0000209biological_processprotein polyubiquitination
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006511biological_processubiquitin-dependent protein catabolic process
B0008270molecular_functionzinc ion binding
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0031466cellular_componentCul5-RING ubiquitin ligase complex
B0031624molecular_functionubiquitin conjugating enzyme binding
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0046872molecular_functionmetal ion binding
B0048588biological_processdevelopmental cell growth
B0061630molecular_functionubiquitin protein ligase activity
B0070534biological_processprotein K63-linked ubiquitination
B0070936biological_processprotein K48-linked ubiquitination
B0071425biological_processhematopoietic stem cell proliferation
B1903955biological_processpositive regulation of protein targeting to mitochondrion
Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CkHdFCwmCL
ChainResidueDetails
ACYS318-LEU327

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues98
DetailsZN_FING: RING-type 1 => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS139-CYS188
BCYS139-CYS188

site_idSWS_FT_FI2
Number of Residues124
DetailsZN_FING: IBR-type => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
AGLU208-CYS270
BGLU208-CYS270

site_idSWS_FT_FI3
Number of Residues58
DetailsZN_FING: RING-type 2; atypical => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS297-CYS326
BCYS297-CYS326

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000305|PubMed:24076655, ECO:0000305|PubMed:31253590
ChainResidueDetails
ACYS310
BCYS310

site_idSWS_FT_FI5
Number of Residues30
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:34518685, ECO:0007744|PDB:7OD1, ECO:0007744|PDB:7ONI
ChainResidueDetails
ACYS139
ACYS249
ACYS252
ACYS257
ACYS260
AHIS265
ACYS270
BCYS139
BCYS142
BCYS156
BHIS158
ACYS142
BCYS161
BCYS183
BCYS188
BCYS228
BCYS233
BCYS249
BCYS252
BCYS257
BCYS260
BHIS265
ACYS156
BCYS270
AHIS158
ACYS161
ACYS183
ACYS188
ACYS228
ACYS233

site_idSWS_FT_FI6
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:34518685, ECO:0007744|PDB:7OD1
ChainResidueDetails
ACYS164
BCYS164
BCYS297
BCYS300
BCYS315
BCYS318
BCYS323
BCYS326
BHIS333
BCYS340
ACYS297
ACYS300
ACYS315
ACYS318
ACYS323
ACYS326
AHIS333
ACYS340

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER353
BSER353

225681

PDB entries from 2024-10-02

PDB statisticsPDBj update infoContact PDBjnumon