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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2WWB

CRYO-EM STRUCTURE OF THE MAMMALIAN SEC61 COMPLEX BOUND TO THE ACTIVELY TRANSLATING WHEAT GERM 80S RIBOSOME

Functional Information from GO Data
ChainGOidnamespacecontents
A0005048molecular_functionsignal sequence binding
A0005784cellular_componentSec61 translocon complex
A0005789cellular_componentendoplasmic reticulum membrane
A0006613biological_processcotranslational protein targeting to membrane
A0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
A0008320molecular_functiontransmembrane protein transporter activity
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0031204biological_processpost-translational protein targeting to membrane, translocation
A0039019biological_processpronephric nephron development
A0043022molecular_functionribosome binding
A0045047biological_processprotein targeting to ER
A0045048biological_processprotein insertion into ER membrane
B0005543molecular_functionphospholipid binding
B0005789cellular_componentendoplasmic reticulum membrane
B0006605biological_processprotein targeting
B0006886biological_processintracellular protein transport
B0008320molecular_functiontransmembrane protein transporter activity
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0022406biological_processmembrane docking
B0031204biological_processpost-translational protein targeting to membrane, translocation
B0043022molecular_functionribosome binding
B0045047biological_processprotein targeting to ER
B0071261cellular_componentSsh1 translocon complex
C0005085molecular_functionguanyl-nucleotide exchange factor activity
C0005783cellular_componentendoplasmic reticulum
C0005784cellular_componentSec61 translocon complex
C0005789cellular_componentendoplasmic reticulum membrane
C0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
C0006886biological_processintracellular protein transport
C0015450molecular_functionprotein-transporting ATPase activity
C0031204biological_processpost-translational protein targeting to membrane, translocation
C0031205cellular_componentendoplasmic reticulum Sec complex
C0043022molecular_functionribosome binding
H0002181biological_processcytoplasmic translation
H0003735molecular_functionstructural constituent of ribosome
H0005634cellular_componentnucleus
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0005840cellular_componentribosome
H0006412biological_processtranslation
H0022625cellular_componentcytosolic large ribosomal subunit
I0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
I0002181biological_processcytoplasmic translation
I0003735molecular_functionstructural constituent of ribosome
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0005840cellular_componentribosome
I0006412biological_processtranslation
I0015934cellular_componentlarge ribosomal subunit
I0022625cellular_componentcytosolic large ribosomal subunit
I0030687cellular_componentpreribosome, large subunit precursor
J0003723molecular_functionRNA binding
J0003735molecular_functionstructural constituent of ribosome
J0005840cellular_componentribosome
J0006412biological_processtranslation
J0022625cellular_componentcytosolic large ribosomal subunit
K0000027biological_processribosomal large subunit assembly
K0002181biological_processcytoplasmic translation
K0003723molecular_functionRNA binding
K0003735molecular_functionstructural constituent of ribosome
K0005515molecular_functionprotein binding
K0005737cellular_componentcytoplasm
K0005829cellular_componentcytosol
K0005840cellular_componentribosome
K0006412biological_processtranslation
K0019843molecular_functionrRNA binding
K0022625cellular_componentcytosolic large ribosomal subunit
K0030687cellular_componentpreribosome, large subunit precursor
L0002181biological_processcytoplasmic translation
L0003723molecular_functionRNA binding
L0003735molecular_functionstructural constituent of ribosome
L0005737cellular_componentcytoplasm
L0005829cellular_componentcytosol
L0005840cellular_componentribosome
L0006412biological_processtranslation
L0015934cellular_componentlarge ribosomal subunit
L0022625cellular_componentcytosolic large ribosomal subunit
L0032991cellular_componentprotein-containing complex
M0002181biological_processcytoplasmic translation
M0003735molecular_functionstructural constituent of ribosome
M0005737cellular_componentcytoplasm
M0005829cellular_componentcytosol
M0005840cellular_componentribosome
M0006412biological_processtranslation
M0006450biological_processregulation of translational fidelity
M0022625cellular_componentcytosolic large ribosomal subunit
N0000463biological_processmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
N0002181biological_processcytoplasmic translation
N0003735molecular_functionstructural constituent of ribosome
N0005737cellular_componentcytoplasm
N0005829cellular_componentcytosol
N0005840cellular_componentribosome
N0006412biological_processtranslation
N0022625cellular_componentcytosolic large ribosomal subunit
N0030687cellular_componentpreribosome, large subunit precursor
O0002181biological_processcytoplasmic translation
O0003735molecular_functionstructural constituent of ribosome
O0005515molecular_functionprotein binding
O0005737cellular_componentcytoplasm
O0005829cellular_componentcytosol
O0005840cellular_componentribosome
O0006412biological_processtranslation
O0022625cellular_componentcytosolic large ribosomal subunit
Functional Information from PROSITE/UniProt
site_idPS00050
Number of Residues16
DetailsRIBOSOMAL_L23 Ribosomal protein L23 signature. KKAYVRLTadydaldI
ChainResidueDetails
KLYS120-ILE135
site_idPS00051
Number of Residues17
DetailsRIBOSOMAL_L39E Ribosomal protein L39e signature. RTnntIryNakrRNWRR
ChainResidueDetails
OARG30-ARG46
site_idPS00464
Number of Residues25
DetailsRIBOSOMAL_L22 Ribosomal protein L22 signature. RrrTyRAhGRinkyesspSHIELvV
ChainResidueDetails
IARG126-VAL150
site_idPS00526
Number of Residues20
DetailsRIBOSOMAL_L19E Ribosomal protein L19e signature. QKRLaAsvvgVGkrkVWLDP
ChainResidueDetails
JGLN7-PRO26
site_idPS00579
Number of Residues15
DetailsRIBOSOMAL_L29 Ribosomal protein L29 signature. SLPKIKtVRKSIACV
ChainResidueDetails
NSER40-VAL54
site_idPS00755
Number of Residues20
DetailsSECY_1 Protein secY signature 1. TLMeLGIsPIVtSGLIMQLL
ChainResidueDetails
ATHR75-LEU94
site_idPS00756
Number of Residues19
DetailsSECY_2 Protein secY signature 2. LLdElLQkgyGLGSGiSLF
ChainResidueDetails
ALEU164-PHE182
site_idPS00939
Number of Residues27
DetailsRIBOSOMAL_L1E Ribosomal protein L1e signature. NhneKryATaSAIaATAvaslvlaRGH
ChainResidueDetails
HASN114-HIS140
site_idPS01067
Number of Residues29
DetailsSECE_SEC61G Protein secE/sec61-gamma signature. FvKDsIrlVkRctKPdrkEfqkiaMATAI
ChainResidueDetails
BPHE14-ILE42
site_idPS01108
Number of Residues18
DetailsRIBOSOMAL_L24 Ribosomal protein L24 signature. DDeVlVVrGskKGqe.GkI
ChainResidueDetails
LASP53-ILE70
site_idPS01144
Number of Residues15
DetailsRIBOSOMAL_L31E Ribosomal protein L31e signature. VRLApeLNqAiWkRG
ChainResidueDetails
MVAL49-GLY63
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues162
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues223
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues151
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"36261528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7TM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7TUT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P60059","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60059","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"1544921","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"26046779","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
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_FI11
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_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues21
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues13
DetailsCompositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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