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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9RSX

Structure of RACK1 bound to the C-terminus of SERBP1 and the RIH region of ZAK

This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKsrNVVI
ChainResidueDetails
N2VAL129-ILE141
site_idPS00548
Number of Residues37
DetailsRIBOSOMAL_S3 Ribosomal protein S3 signature. AKsmkfvdGlMihSgdpVnyyVDtavrhvlLrqGvlG
ChainResidueDetails
RDALA147-GLY183
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ALSGswDgTLRLWDL
ChainResidueDetails
RgALA78-LEU92
RgILE120-THR134
RgILE165-LEU179
RgCYS207-LEU221
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1 and PKC/PRKCD","evidences":[{"source":"PubMed","id":"19059439","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21871177","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16807684","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues31
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues30
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues30
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues32
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues30
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues29
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues30
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2006","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Kanor S.","Tissot J.-D.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by ABL1","evidences":[{"source":"PubMed","id":"19423701","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P68040","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"11279199","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase","evidences":[{"source":"PubMed","id":"28636603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P68040","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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