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1LDJ

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0006915biological_processapoptotic process
A0008283biological_processcell population proliferation
A0009887biological_processanimal organ morphogenesis
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031461cellular_componentcullin-RING ubiquitin ligase complex
A0031625molecular_functionubiquitin protein ligase binding
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0070936biological_processprotein K48-linked ubiquitination
A0097193biological_processintrinsic apoptotic signaling pathway
A0160072molecular_functionubiquitin ligase complex scaffold activity
A1990452cellular_componentParkin-FBXW7-Cul1 ubiquitin ligase complex
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 201
ChainResidue
BCYS42
BCYS45
BHIS80
BCYS83

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 202
ChainResidue
BCYS75
BHIS77
BCYS94
BASP97

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 203
ChainResidue
BCYS56
BCYS68
BHIS82
BCYS53

Functional Information from PROSITE/UniProt
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKkcIdiLIEKeYLeRvdgekdtYsYlA
ChainResidueDetails
AILE749-ALA776

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues45
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
BCYS53-ASN98

site_idSWS_FT_FI2
Number of Residues11
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
BCYS42
BCYS94
BASP97
BCYS45
BCYS53
BCYS56
BCYS68
BCYS75
BHIS77
BHIS80
BHIS82

site_idSWS_FT_FI3
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
BCYS83

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PDB entries from 2024-07-24

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