Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7VGG

Cryo-EM structure of Ultraviolet-B activated UVR8 in complex with COP1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000152cellular_componentnuclear ubiquitin ligase complex
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0008270molecular_functionzinc ion binding
A0009585biological_processred, far-red light phototransduction
A0009640biological_processphotomorphogenesis
A0009641biological_processshade avoidance
A0009647biological_processskotomorphogenesis
A0009649biological_processentrainment of circadian clock
A0009963biological_processpositive regulation of flavonoid biosynthetic process
A0010017biological_processred or far-red light signaling pathway
A0010119biological_processregulation of stomatal movement
A0010224biological_processresponse to UV-B
A0016567biological_processprotein ubiquitination
A0016604cellular_componentnuclear body
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0046283biological_processanthocyanin-containing compound metabolic process
A0046872molecular_functionmetal ion binding
A0048573biological_processphotoperiodism, flowering
A0061630molecular_functionubiquitin protein ligase activity
A0080008cellular_componentCul4-RING E3 ubiquitin ligase complex
B0000785cellular_componentchromatin
B0003682molecular_functionchromatin binding
B0005085molecular_functionguanyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009411biological_processresponse to UV
B0009536cellular_componentplastid
B0009649biological_processentrainment of circadian clock
B0009881molecular_functionphotoreceptor activity
B0010224biological_processresponse to UV-B
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CgHsFCymCI
ChainResidueDetails
ACYS67-ILE76

site_idPS00626
Number of Residues11
DetailsRCC1_2 Regulator of chromosome condensation (RCC1) signature 2. ISAGaSHSVAL
ChainResidueDetails
BILE20-LEU30
BVAL177-VAL187
BVAL229-VAL239
BILE281-LEU291
BVAL333-VAL343

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LASAstDsTLRLWDV
ChainResidueDetails
ALEU563-VAL577

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsRepeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsRepeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues38
DetailsRepeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues39
DetailsRepeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsRegion: {"description":"Binding of human TRIB1 COP1-binding-motif","evidences":[{"source":"PubMed","id":"27041596","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Human TRIB1 COP1-binding motif","evidences":[{"source":"PubMed","id":"27041596","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues52
DetailsRepeat: {"description":"RCC1 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues51
DetailsRepeat: {"description":"RCC1 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues50
DetailsRepeat: {"description":"RCC1 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues51
DetailsRepeat: {"description":"RCC1 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues50
DetailsRepeat: {"description":"RCC1 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues51
DetailsRepeat: {"description":"RCC1 7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

PDB statisticsPDBj update infoContact PDBjnumon