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2AST

Crystal structure of Skp1-Skp2-Cks1 in complex with a p27 peptide

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
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
A0070936biological_processprotein K48-linked ubiquitination
A0097602molecular_functioncullin family protein binding
A0140677molecular_functionmolecular function activator activity
A0160072molecular_functionubiquitin ligase complex scaffold activity
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 Residues7
DetailsBINDING SITE FOR RESIDUE BEN C 1001
ChainResidue
BPHE2169
BVAL2192
CHOH100
CHOH182
CHOH247
CMET3058
CARG3070

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE BEN B 1002
ChainResidue
BHOH263
BALA2227
BSER2230
BSER2254
CHIS3021
CHIS3060
CGLU3063
CILE3066
BHOH67
BHOH74

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR CHAIN D OF CYCLIN-DEPENDENT KINASE INHIBITOR 1B
ChainResidue
BHOH13
BARG2294
BTYR2346
BASP2347
CTYR3008
CASP3010
CLYS3011
CARG3020
CARG3044
CGLN3049
CGLN3050
CSER3051
CGLN3052
CTRP3054

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

242842

PDB entries from 2025-10-08

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