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

2ASS

Crystal structure of the Skp1-Skp2-Cks1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006511biological_processubiquitin-dependent protein catabolic process
A0006513biological_processprotein monoubiquitination
A0006915biological_processapoptotic process
A0008013molecular_functionbeta-catenin binding
A0016567biological_processprotein ubiquitination
A0019005cellular_componentSCF ubiquitin ligase complex
A0019904molecular_functionprotein domain specific binding
A0031146biological_processSCF-dependent proteasomal ubiquitin-dependent protein catabolic process
A0031467cellular_componentCul7-RING ubiquitin ligase complex
A0031519cellular_componentPcG protein complex
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0051457biological_processmaintenance of protein location in nucleus
A0061564biological_processaxon development
A0070936biological_processprotein K48-linked ubiquitination
A0097602molecular_functioncullin family protein binding
A0140677molecular_functionmolecular function activator activity
A0160072molecular_functionubiquitin ligase complex scaffold activity
A1904037biological_processpositive regulation of epithelial cell apoptotic process
A1990444molecular_functionF-box domain binding
A1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
A1990757molecular_functionubiquitin ligase activator activity
C0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 3
ChainResidue
BHOH67
BHIS2199
BSER2203
BTHR2225
CPRO3062

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 C 4
ChainResidue
CSER3051
CTRP3054
CHOH72
CLYS3011
CARG3020
CGLN3050

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 5
ChainResidue
BASN2190
BGLU2214
BGLY2215
CLEU3037
CMET3038
CSER3039
CHIS3056

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEN B 1
ChainResidue
BHOH22
BHOH38
BALA2227
BSER2254
CHIS3060
CGLU3063

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BEN C 2
ChainResidue
BPHE2169
BVAL2192
CTYR3057
CMET3058

Functional Information from PROSITE/UniProt
site_idPS00944
Number of Residues19
DetailsCKS_1 Cyclin-dependent kinases regulatory subunits signature 1. YSdKYdDEeFEYRHVmLPK
ChainResidueDetails
CTYR3008-LYS3026

site_idPS00945
Number of Residues11
DetailsCKS_2 Cyclin-dependent kinases regulatory subunits signature 2. HePEpHILLFR
ChainResidueDetails
CHIS3060-ARG3070

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues25
DetailsRepeat: {"description":"LRR 1","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues27
DetailsRepeat: {"description":"LRR 2","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues24
DetailsRepeat: {"description":"LRR 3","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsRepeat: {"description":"LRR 4","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues26
DetailsRepeat: {"description":"LRR 5","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsRepeat: {"description":"LRR 6","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsRepeat: {"description":"LRR 7","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues22
DetailsRepeat: {"description":"LRR 8","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues19
DetailsRepeat: {"description":"LRR 9","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues21
DetailsRepeat: {"description":"LRR 10","evidences":[{"source":"PubMed","id":"11099048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon