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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4V4B

Structure of the ribosomal 80S-eEF2-sordarin complex from yeast obtained by docking atomic models for RNA and protein components into a 11.7 A cryo-EM map.

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AB0003735molecular_functionstructural constituent of ribosome
AB0005840cellular_componentribosome
AB0006412biological_processtranslation
AB0015935cellular_componentsmall ribosomal subunit
AC0003723molecular_functionRNA binding
AC0003735molecular_functionstructural constituent of ribosome
AC0006412biological_processtranslation
AC0015935cellular_componentsmall ribosomal subunit
AD0000462biological_processmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
AD0003723molecular_functionRNA binding
AD0003735molecular_functionstructural constituent of ribosome
AD0005515molecular_functionprotein binding
AD0005654cellular_componentnucleoplasm
AD0005730cellular_componentnucleolus
AD0005737cellular_componentcytoplasm
AD0005829cellular_componentcytosol
AD0005840cellular_componentribosome
AD0006364biological_processrRNA processing
AD0006412biological_processtranslation
AD0015935cellular_componentsmall ribosomal subunit
AD0019843molecular_functionrRNA binding
AD0022627cellular_componentcytosolic small ribosomal subunit
AD0030476biological_processascospore wall assembly
AD0030686cellular_component90S preribosome
AD0032040cellular_componentsmall-subunit processome
AD0042254biological_processribosome biogenesis
AD0042274biological_processribosomal small subunit biogenesis
AD1990904cellular_componentribonucleoprotein complex
AE0003723molecular_functionRNA binding
AE0003735molecular_functionstructural constituent of ribosome
AE0005840cellular_componentribosome
AE0006412biological_processtranslation
AE0015935cellular_componentsmall ribosomal subunit
AG0003723molecular_functionRNA binding
AG0003735molecular_functionstructural constituent of ribosome
AG0006412biological_processtranslation
AG0015935cellular_componentsmall ribosomal subunit
AH0003735molecular_functionstructural constituent of ribosome
AH0005840cellular_componentribosome
AH0006412biological_processtranslation
AI0003735molecular_functionstructural constituent of ribosome
AI0005840cellular_componentribosome
AI0006412biological_processtranslation
AJ0003723molecular_functionRNA binding
AJ0003735molecular_functionstructural constituent of ribosome
AJ0005840cellular_componentribosome
AJ0006412biological_processtranslation
AJ0015935cellular_componentsmall ribosomal subunit
AK0000028biological_processribosomal small subunit assembly
AK0000462biological_processmaturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
AK0002181biological_processcytoplasmic translation
AK0003729molecular_functionmRNA binding
AK0003735molecular_functionstructural constituent of ribosome
AK0005654cellular_componentnucleoplasm
AK0005730cellular_componentnucleolus
AK0005737cellular_componentcytoplasm
AK0005829cellular_componentcytosol
AK0005840cellular_componentribosome
AK0006364biological_processrRNA processing
AK0006412biological_processtranslation
AK0022627cellular_componentcytosolic small ribosomal subunit
AK0030686cellular_component90S preribosome
AK0032040cellular_componentsmall-subunit processome
AK0042254biological_processribosome biogenesis
AK1990904cellular_componentribonucleoprotein complex
AL0003735molecular_functionstructural constituent of ribosome
AL0005840cellular_componentribosome
AL0006412biological_processtranslation
AL0015935cellular_componentsmall ribosomal subunit
AM0003676molecular_functionnucleic acid binding
AM0003723molecular_functionRNA binding
AM0003735molecular_functionstructural constituent of ribosome
AM0005840cellular_componentribosome
AM0006412biological_processtranslation
AN0003735molecular_functionstructural constituent of ribosome
AN0005840cellular_componentribosome
AN0006412biological_processtranslation
AN0008270molecular_functionzinc ion binding
AO0003735molecular_functionstructural constituent of ribosome
AO0005840cellular_componentribosome
AO0006412biological_processtranslation
AQ0003735molecular_functionstructural constituent of ribosome
AQ0005840cellular_componentribosome
AQ0006412biological_processtranslation
AS0003723molecular_functionRNA binding
AS0003735molecular_functionstructural constituent of ribosome
AS0005840cellular_componentribosome
AS0006412biological_processtranslation
AT0000166molecular_functionnucleotide binding
AT0003723molecular_functionRNA binding
AT0003746molecular_functiontranslation elongation factor activity
AT0003924molecular_functionGTPase activity
AT0005515molecular_functionprotein binding
AT0005525molecular_functionGTP binding
AT0005737cellular_componentcytoplasm
AT0005829cellular_componentcytosol
AT0006412biological_processtranslation
AT0006414biological_processtranslational elongation
AT0016787molecular_functionhydrolase activity
AT0019843molecular_functionrRNA binding
AT0042802molecular_functionidentical protein binding
AT0043022molecular_functionribosome binding
AT0045901biological_processpositive regulation of translational elongation
AT0051087molecular_functionprotein-folding chaperone binding
AT1990145biological_processmaintenance of translational fidelity
AT1990904cellular_componentribonucleoprotein complex
B00002181biological_processcytoplasmic translation
B00003735molecular_functionstructural constituent of ribosome
B00005737cellular_componentcytoplasm
B00005829cellular_componentcytosol
B00005840cellular_componentribosome
B00006412biological_processtranslation
B00022625cellular_componentcytosolic large ribosomal subunit
B01990904cellular_componentribonucleoprotein complex
B90003735molecular_functionstructural constituent of ribosome
B90005840cellular_componentribosome
B90006412biological_processtranslation
BA0003723molecular_functionRNA binding
BA0003735molecular_functionstructural constituent of ribosome
BA0006412biological_processtranslation
BA0015934cellular_componentlarge ribosomal subunit
BB0003735molecular_functionstructural constituent of ribosome
BB0005840cellular_componentribosome
BB0006412biological_processtranslation
BC0000027biological_processribosomal large subunit assembly
BC0002181biological_processcytoplasmic translation
BC0003723molecular_functionRNA binding
BC0003735molecular_functionstructural constituent of ribosome
BC0005515molecular_functionprotein binding
BC0005737cellular_componentcytoplasm
BC0005829cellular_componentcytosol
BC0005840cellular_componentribosome
BC0006364biological_processrRNA processing
BC0006412biological_processtranslation
BC0006414biological_processtranslational elongation
BC0022625cellular_componentcytosolic large ribosomal subunit
BC1990145biological_processmaintenance of translational fidelity
BC1990904cellular_componentribonucleoprotein complex
BD0002181biological_processcytoplasmic translation
BD0003723molecular_functionRNA binding
BD0003735molecular_functionstructural constituent of ribosome
BD0005634cellular_componentnucleus
BD0005737cellular_componentcytoplasm
BD0005829cellular_componentcytosol
BD0005840cellular_componentribosome
BD0006412biological_processtranslation
BD0022625cellular_componentcytosolic large ribosomal subunit
BD1990904cellular_componentribonucleoprotein complex
BE0003735molecular_functionstructural constituent of ribosome
BE0005840cellular_componentribosome
BE0006412biological_processtranslation
BE0008097molecular_function5S rRNA binding
BF0003723molecular_functionRNA binding
BG0003723molecular_functionRNA binding
BG0042254biological_processribosome biogenesis
BG1990904cellular_componentribonucleoprotein complex
BH0002181biological_processcytoplasmic translation
BH0003735molecular_functionstructural constituent of ribosome
BH0005515molecular_functionprotein binding
BH0005737cellular_componentcytoplasm
BH0005829cellular_componentcytosol
BH0005840cellular_componentribosome
BH0006412biological_processtranslation
BH0019843molecular_functionrRNA binding
BH0022625cellular_componentcytosolic large ribosomal subunit
BH1990904cellular_componentribonucleoprotein complex
BI0003735molecular_functionstructural constituent of ribosome
BI0005840cellular_componentribosome
BI0006412biological_processtranslation
BJ0003735molecular_functionstructural constituent of ribosome
BJ0005840cellular_componentribosome
BJ0006412biological_processtranslation
BK0003735molecular_functionstructural constituent of ribosome
BK0005840cellular_componentribosome
BK0006412biological_processtranslation
BL0000470biological_processmaturation of LSU-rRNA
BL0002181biological_processcytoplasmic translation
BL0003723molecular_functionRNA binding
BL0003735molecular_functionstructural constituent of ribosome
BL0005737cellular_componentcytoplasm
BL0005829cellular_componentcytosol
BL0005840cellular_componentribosome
BL0006412biological_processtranslation
BL0022625cellular_componentcytosolic large ribosomal subunit
BL0180023biological_processcytosolic large ribosomal subunit assembly
BL1990904cellular_componentribonucleoprotein complex
BM0003735molecular_functionstructural constituent of ribosome
BM0005840cellular_componentribosome
BM0006412biological_processtranslation
BM0015934cellular_componentlarge ribosomal subunit
BN0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
BN0002181biological_processcytoplasmic translation
BN0003735molecular_functionstructural constituent of ribosome
BN0005737cellular_componentcytoplasm
BN0005829cellular_componentcytosol
BN0005840cellular_componentribosome
BN0006412biological_processtranslation
BN0015934cellular_componentlarge ribosomal subunit
BN0022625cellular_componentcytosolic large ribosomal subunit
BN0030687cellular_componentpreribosome, large subunit precursor
BN1990904cellular_componentribonucleoprotein complex
BO0003735molecular_functionstructural constituent of ribosome
BO0005840cellular_componentribosome
BO0006412biological_processtranslation
BP0003723molecular_functionRNA binding
BP0003735molecular_functionstructural constituent of ribosome
BP0005840cellular_componentribosome
BP0006412biological_processtranslation
BP0022625cellular_componentcytosolic large ribosomal subunit
BQ0003735molecular_functionstructural constituent of ribosome
BQ0005840cellular_componentribosome
BQ0006412biological_processtranslation
BR0003735molecular_functionstructural constituent of ribosome
BR0005840cellular_componentribosome
BR0006412biological_processtranslation
BS0003735molecular_functionstructural constituent of ribosome
BT0003735molecular_functionstructural constituent of ribosome
BT0005840cellular_componentribosome
BT0006412biological_processtranslation
BT0019843molecular_functionrRNA binding
BU0002181biological_processcytoplasmic translation
BU0003723molecular_functionRNA binding
BU0003735molecular_functionstructural constituent of ribosome
BU0005737cellular_componentcytoplasm
BU0005829cellular_componentcytosol
BU0005840cellular_componentribosome
BU0006412biological_processtranslation
BU0015934cellular_componentlarge ribosomal subunit
BU0022625cellular_componentcytosolic large ribosomal subunit
BU0032991cellular_componentprotein-containing complex
BU0042273biological_processribosomal large subunit biogenesis
BU1990904cellular_componentribonucleoprotein complex
BV0002181biological_processcytoplasmic translation
BV0003723molecular_functionRNA binding
BV0003735molecular_functionstructural constituent of ribosome
BV0005634cellular_componentnucleus
BV0005737cellular_componentcytoplasm
BV0005829cellular_componentcytosol
BV0005840cellular_componentribosome
BV0006412biological_processtranslation
BV0015934cellular_componentlarge ribosomal subunit
BV0022625cellular_componentcytosolic large ribosomal subunit
BV1990904cellular_componentribonucleoprotein complex
BW0003735molecular_functionstructural constituent of ribosome
BW0005840cellular_componentribosome
BW0006412biological_processtranslation
BX0000463biological_processmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
BX0003735molecular_functionstructural constituent of ribosome
BX0005840cellular_componentribosome
BX0006412biological_processtranslation
BX0022625cellular_componentcytosolic large ribosomal subunit
BY0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
BY0002181biological_processcytoplasmic translation
BY0003723molecular_functionRNA binding
BY0003735molecular_functionstructural constituent of ribosome
BY0005515molecular_functionprotein binding
BY0005737cellular_componentcytoplasm
BY0005829cellular_componentcytosol
BY0005840cellular_componentribosome
BY0006412biological_processtranslation
BY0008270molecular_functionzinc ion binding
BY0019843molecular_functionrRNA binding
BY0022625cellular_componentcytosolic large ribosomal subunit
BY0030687cellular_componentpreribosome, large subunit precursor
BY0046872molecular_functionmetal ion binding
BY1990904cellular_componentribonucleoprotein complex
BZ0003735molecular_functionstructural constituent of ribosome
BZ0005840cellular_componentribosome
BZ0006412biological_processtranslation
Functional Information from PROSITE/UniProt
site_idPS00049
Number of Residues27
DetailsRIBOSOMAL_L14 Ribosomal protein L14 signature. AIVVrqakswrrr.DGvflyFedNagVI
ChainResidueDetails
BRALA76-ILE102
site_idPS00050
Number of Residues16
DetailsRIBOSOMAL_L23 Ribosomal protein L23 signature. KKAYVRLTadydaldI
ChainResidueDetails
BTLYS119-ILE134
site_idPS00052
Number of Residues27
DetailsRIBOSOMAL_S7 Ribosomal protein S7 signature. ErLtnsLMmngrnnGKKlkavrIIkhT
ChainResidueDetails
AGGLU90-THR116
site_idPS00053
Number of Residues18
DetailsRIBOSOMAL_S8 Ribosomal protein S8 signature. GyvILTTSaGIMdheeAR
ChainResidueDetails
AHGLY99-ARG116
site_idPS00054
Number of Residues23
DetailsRIBOSOMAL_S11 Ribosomal protein S11 signature. LrALarS.GLrIgrieDvTPvPSD
ChainResidueDetails
AKLEU101-ASP123
site_idPS00055
Number of Residues8
DetailsRIBOSOMAL_S12 Ribosomal protein S12 signature. KqPNSAiR
ChainResidueDetails
ALLYS62-ARG69
site_idPS00056
Number of Residues13
DetailsRIBOSOMAL_S17 Ribosomal protein S17 signature. GDiVtVgQcRPIS
ChainResidueDetails
AQGLY119-SER131
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DTrkdEQeRGITIksT
ChainResidueDetails
ATASP58-THR73
site_idPS00323
Number of Residues25
DetailsRIBOSOMAL_S19 Ribosomal protein S19 signature. NGKafnqveIrpemLGhyLGEFsiT
ChainResidueDetails
ASASN98-THR122
site_idPS00358
Number of Residues17
DetailsRIBOSOMAL_L5 Ribosomal protein L5 signature. LeqLSGQtpVqSkARyT
ChainResidueDetails
BJLEU36-THR52
site_idPS00360
Number of Residues19
DetailsRIBOSOMAL_S9 Ribosomal protein S9 signature. GGGhvSQvyAirqAiAKGL
ChainResidueDetails
AIGLY70-LEU88
site_idPS00361
Number of Residues16
DetailsRIBOSOMAL_S10 Ribosomal protein S10 signature. AeqhNLvkkGPVrLPT
ChainResidueDetails
AJALA45-THR60
site_idPS00362
Number of Residues31
DetailsRIBOSOMAL_S15 Ribosomal protein S15 signature. VrkHLernRkDkdAkfrLilIesrihrLarY
ChainResidueDetails
AOVAL97-TYR127
site_idPS00464
Number of Residues25
DetailsRIBOSOMAL_L22 Ribosomal protein L22 signature. RrrTyRAhGRinkyesspSHIELvV
ChainResidueDetails
BNARG125-VAL149
site_idPS00467
Number of Residues12
DetailsRIBOSOMAL_L2 Ribosomal protein L2 signature. PktRGVAmNPvD
ChainResidueDetails
BBPRO196-ASP207
site_idPS00474
Number of Residues24
DetailsRIBOSOMAL_L3 Ribosomal protein L3 signature. FeqnemiDaiAvTkGHGfeGvthR
ChainResidueDetails
BCPHE208-ARG231
site_idPS00475
Number of Residues32
DetailsRIBOSOMAL_L15 Ribosomal protein L15 signature. KILGkGrIpnvp.ViVkarfVSklAeekIraaG
ChainResidueDetails
BVLYS110-GLY141
site_idPS00526
Number of Residues20
DetailsRIBOSOMAL_L19E Ribosomal protein L19e signature. QKRLaAsvvgVGkrkVWLDP
ChainResidueDetails
BPGLN6-PRO25
site_idPS00527
Number of Residues23
DetailsRIBOSOMAL_S14 Ribosomal protein S14 signature. RvCsshtglvrkyd.LNICRqCFR
ChainResidueDetails
ANARG21-ARG43
site_idPS00548
Number of Residues37
DetailsRIBOSOMAL_S3 Ribosomal protein S3 signature. AKamkfadGfLihSgqpVndfIDtatrhvlMrqGvlG
ChainResidueDetails
ACALA146-GLY182
site_idPS00579
Number of Residues15
DetailsRIBOSOMAL_L29 Ribosomal protein L29 signature. SLPKIKtVRKSIACV
ChainResidueDetails
BXSER40-VAL54
site_idPS00580
Number of Residues21
DetailsRIBOSOMAL_L32E Ribosomal protein L32e signature. FkRhhsdRyhRVaen..WRKqkG
ChainResidueDetails
B0PHE17-GLY37
site_idPS00585
Number of Residues33
DetailsRIBOSOMAL_S5 Ribosomal protein S5 signature. GQrtrFkAvvVVGDsn.GhVGlGiktak.EVag.AI
ChainResidueDetails
AEGLY92-ILE124
site_idPS00632
Number of Residues25
DetailsRIBOSOMAL_S4 Ribosomal protein S4 signature. LErRLqtqVYKlglAkSvhhARvLI
ChainResidueDetails
ADLEU105-ILE129
site_idPS00634
Number of Residues33
DetailsRIBOSOMAL_L30 Ribosomal protein L30 signature. VLqlLrLtRinSgTfvkvtkatleLLklIepYV
ChainResidueDetails
BFVAL101-VAL133
site_idPS00646
Number of Residues14
DetailsRIBOSOMAL_S13_1 Ribosomal protein S13 signature. RGiRHfwGlrVRGQ
ChainResidueDetails
AMARG123-GLN136
site_idPS00700
Number of Residues22
DetailsRIBOSOMAL_L6_2 Ribosomal protein L6 signature 2. QicrVrnKdiRkFlDGIYVshK
ChainResidueDetails
BHGLN163-LYS184
site_idPS00783
Number of Residues24
DetailsRIBOSOMAL_L13 Ribosomal protein L13 signature. LRGMVShktarGKaalerLkVFeG
ChainResidueDetails
BMLEU83-GLY106
site_idPS00939
Number of Residues27
DetailsRIBOSOMAL_L1E Ribosomal protein L1e signature. NhneKryATaSAIaATAvaslvlaRGH
ChainResidueDetails
BDASN113-HIS139
site_idPS00962
Number of Residues12
DetailsRIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. AqLLLAANTHLG
ChainResidueDetails
ABALA13-GLY24
site_idPS00963
Number of Residues25
DetailsRIBOSOMAL_S2_2 Ribosomal protein S2 signature 2. PrlVIVtDprsDaqaIkEasyvNIP
ChainResidueDetails
ABPRO117-PRO141
site_idPS01073
Number of Residues18
DetailsRIBOSOMAL_L24E Ribosomal protein L24e signature. FsGakIyPGrGtlFvRgD
ChainResidueDetails
BSPHE8-ASP25
site_idPS01077
Number of Residues20
DetailsRIBOSOMAL_L37E Ribosomal protein L37e signature. GTpSfGkRhnks.HtlCnRCG
ChainResidueDetails
BYGLY3-GLY22
site_idPS01082
Number of Residues18
DetailsRIBOSOMAL_L7AE Ribosomal protein L7Ae signature. CkkmgVPYaiVkGKarLG
ChainResidueDetails
BGCYS169-GLY186
site_idPS01106
Number of Residues18
DetailsRIBOSOMAL_L18E Ribosomal protein L18e signature. KaLflSKinRPpVSVsRI
ChainResidueDetails
BOLYS50-ILE67
site_idPS01108
Number of Residues18
DetailsRIBOSOMAL_L24 Ribosomal protein L24 signature. DDeVlVVrGskKGqe.GkI
ChainResidueDetails
BUASP53-ILE70
site_idPS01144
Number of Residues15
DetailsRIBOSOMAL_L31E Ribosomal protein L31e signature. VRLApeLNqAiWkRG
ChainResidueDetails
BWVAL48-GLY62
site_idPS01171
Number of Residues26
DetailsRIBOSOMAL_L21E Ribosomal protein L21e signature. GDiVdikangsiqk.GmpHkfYqGkTG
ChainResidueDetails
BQGLY37-GLY62
site_idPS01172
Number of Residues12
DetailsRIBOSOMAL_L44E Ribosomal protein L44e signature. KtTKKvvLRleC
ChainResidueDetails
BZLYS62-CYS73
site_idPS01194
Number of Residues24
DetailsRIBOSOMAL_L15E Ribosomal protein L15e signature. DKARrLGYkAkqGFVIYRvRVrRG
ChainResidueDetails
BLASP45-GLY68
site_idPS01199
Number of Residues20
DetailsRIBOSOMAL_L1 Ribosomal protein L1 signature. IkqVprlLGpqLSKAGkFPT
ChainResidueDetails
BAILE117-THR136
site_idPS01257
Number of Residues22
DetailsRIBOSOMAL_L10E Ribosomal protein L10e signature. ADRlqqGMRgAWGKPhGlaARV
ChainResidueDetails
BIALA108-VAL129
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17082187","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NPF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17082187","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1U2R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2E1R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NPF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; by EFM3; alternate","evidences":[{"source":"PubMed","id":"24517342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25086354","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues13
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; by EFM2; alternate","evidences":[{"source":"PubMed","id":"24517342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25086354","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Diphthamide","evidences":[{"source":"PubMed","id":"15316019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16950777","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"721806","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues57
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues71
DetailsDomain: {"description":"KH type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00118","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues10
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine; by SFM1","evidences":[{"source":"PubMed","id":"22650761","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues74
DetailsDomain: {"description":"S4 RNA-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00182","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05755","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P05755","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues63
DetailsDomain: {"description":"S5 DRBM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00268","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues68
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues43
DetailsCompositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"3,4-dihydroxyproline","evidences":[{"source":"PubMed","id":"24550462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; by RKM1","evidences":[{"source":"PubMed","id":"22522802","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; by RKM5","evidences":[{"source":"PubMed","id":"21460220","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Pros-methylhistidine","evidences":[{"source":"PubMed","id":"20864530","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24865971","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26826131","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"26046779","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues2
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"22522802","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"N5-methylarginine; by RMT2","evidences":[{"source":"PubMed","id":"11856739","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18957409","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"1544921","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q12672","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues2
DetailsModified residue: {"description":"N6,N6-dimethyllysine; by RKM1","evidences":[{"source":"PubMed","id":"17327221","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P24000","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"15542864","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues12
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"source":"PubMed","id":"2104804","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues18
DetailsZinc finger: {"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22096102","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; by RKM3","evidences":[{"source":"PubMed","id":"18957409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22522802","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24517342","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; by RKM4","evidences":[{"source":"PubMed","id":"18957409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24517342","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues21
DetailsZinc finger: {"description":"C4-type"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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