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2LGV

Rbx1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0006974biological_processDNA damage response
A0007283biological_processspermatogenesis
A0008270molecular_functionzinc ion binding
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0019005cellular_componentSCF ubiquitin ligase complex
A0019788molecular_functionNEDD8 transferase activity
A0030163biological_processprotein catabolic process
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031461cellular_componentcullin-RING ubiquitin ligase complex
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0031463cellular_componentCul3-RING ubiquitin ligase complex
A0031464cellular_componentCul4A-RING E3 ubiquitin ligase complex
A0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
A0031466cellular_componentCul5-RING ubiquitin ligase complex
A0031467cellular_componentCul7-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032480biological_processnegative regulation of type I interferon production
A0034450molecular_functionubiquitin-ubiquitin ligase activity
A0034644biological_processcellular response to UV
A0042110biological_processT cell activation
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0043687biological_processpost-translational protein modification
A0045116biological_processprotein neddylation
A0045732biological_processpositive regulation of protein catabolic process
A0046872molecular_functionmetal ion binding
A0060090molecular_functionmolecular adaptor activity
A0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
A0061630molecular_functionubiquitin protein ligase activity
A0061663molecular_functionNEDD8 ligase activity
A0062197biological_processcellular response to chemical stress
A0070936biological_processprotein K48-linked ubiquitination
A0071230biological_processcellular response to amino acid stimulus
A0090090biological_processnegative regulation of canonical Wnt signaling pathway
A0097602molecular_functioncullin family protein binding
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A1900076biological_processregulation of cellular response to insulin stimulus
A1902499biological_processpositive regulation of protein autoubiquitination
A1902883biological_processnegative regulation of response to oxidative stress
A1904263biological_processpositive regulation of TORC1 signaling
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 109
ChainResidue
ACYS42
ACYS45
AHIS80
ACYS83

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 110
ChainResidue
ACYS53
ACYS56
ACYS68
AHIS82

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 111
ChainResidue
AHIS77
ACYS94
AASP97
ACYS75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues45
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
ACYS53-ASN98

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
ChainResidueDetails
ACYS42
ACYS45
ACYS75
AHIS77
AHIS80
ACYS94
AASP97

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O, ECO:0007744|PDB:7Z8B
ChainResidueDetails
ACYS53
ACYS56
ACYS68
AHIS82

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
ChainResidueDetails
ACYS83

226707

PDB entries from 2024-10-30

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