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3J46

Structure of the SecY protein translocation channel in action

Functional Information from GO Data
ChainGOidnamespacecontents
50000027biological_processribosomal large subunit assembly
50000049molecular_functiontRNA binding
50002181biological_processcytoplasmic translation
50003723molecular_functionRNA binding
50003729molecular_functionmRNA binding
50003735molecular_functionstructural constituent of ribosome
50005515molecular_functionprotein binding
50005737cellular_componentcytoplasm
50005829cellular_componentcytosol
50005840cellular_componentribosome
50006412biological_processtranslation
50006417biological_processregulation of translation
50015934cellular_componentlarge ribosomal subunit
50019843molecular_functionrRNA binding
50022625cellular_componentcytosolic large ribosomal subunit
50045947biological_processnegative regulation of translational initiation
51990904cellular_componentribonucleoprotein complex
E0006605biological_processprotein targeting
E0006886biological_processintracellular protein transport
E0008320molecular_functionprotein transmembrane transporter activity
E0009306biological_processprotein secretion
E0016020cellular_componentmembrane
G0009306biological_processprotein secretion
G0015450molecular_functionprotein-transporting ATPase activity
G0016020cellular_componentmembrane
T0000027biological_processribosomal large subunit assembly
T0002181biological_processcytoplasmic translation
T0003723molecular_functionRNA binding
T0003735molecular_functionstructural constituent of ribosome
T0005515molecular_functionprotein binding
T0005737cellular_componentcytoplasm
T0005840cellular_componentribosome
T0006412biological_processtranslation
T0019843molecular_functionrRNA binding
T0022625cellular_componentcytosolic large ribosomal subunit
T1990904cellular_componentribonucleoprotein complex
U0000027biological_processribosomal large subunit assembly
U0002181biological_processcytoplasmic translation
U0003723molecular_functionRNA binding
U0003735molecular_functionstructural constituent of ribosome
U0005515molecular_functionprotein binding
U0005737cellular_componentcytoplasm
U0005829cellular_componentcytosol
U0005840cellular_componentribosome
U0006412biological_processtranslation
U0019843molecular_functionrRNA binding
U0022625cellular_componentcytosolic large ribosomal subunit
U0070180molecular_functionlarge ribosomal subunit rRNA binding
U1990904cellular_componentribonucleoprotein complex
y0005048molecular_functionsignal sequence binding
y0005515molecular_functionprotein binding
y0005886cellular_componentplasma membrane
y0006605biological_processprotein targeting
y0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
y0006886biological_processintracellular protein transport
y0008320molecular_functionprotein transmembrane transporter activity
y0015031biological_processprotein transport
y0016020cellular_componentmembrane
y0031522cellular_componentcell envelope Sec protein transport complex
y0043952biological_processprotein transport by the Sec complex
y0065002biological_processintracellular protein transmembrane transport
Y0000027biological_processribosomal large subunit assembly
Y0002181biological_processcytoplasmic translation
Y0003723molecular_functionRNA binding
Y0003735molecular_functionstructural constituent of ribosome
Y0005737cellular_componentcytoplasm
Y0005840cellular_componentribosome
Y0006412biological_processtranslation
Y0019843molecular_functionrRNA binding
Y0022625cellular_componentcytosolic large ribosomal subunit
Y1990904cellular_componentribonucleoprotein complex
Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues66
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mireerllkvlraphvsekastameksntivlkvakdatkaeikaavqklfevevevv.........................................................NTLVVKGK
ChainResidueDetails
TMET1-LYS66

site_idPS00579
Number of Residues15
DetailsRIBOSOMAL_L29 Ribosomal protein L29 signature. QSHLLKqVRRDVARV
ChainResidueDetails
YGLN39-VAL53

site_idPS01199
Number of Residues19
DetailsRIBOSOMAL_L1 Ribosomal protein L1 signature. MrvVgq.LGqvLGPRGlMPN
ChainResidueDetails
5MET121-ASN139

site_idPS01108
Number of Residues18
DetailsRIBOSOMAL_L24 Ribosomal protein L24 signature. DDeViVLtGkdKGkr.GkV
ChainResidueDetails
UASP7-VAL24

site_idPS00755
Number of Residues20
DetailsSECY_1 Protein secY signature 1. SIFaLGImPYIsASIIIQLL
ChainResidueDetails
ySER76-LEU95

site_idPS00756
Number of Residues18
DetailsSECY_2 Protein secY signature 2. WLgEqITer.GIGNGiSII
ChainResidueDetails
yTRP173-ILE190

site_idPS00050
Number of Residues16
DetailsRIBOSOMAL_L23 Ribosomal protein L23 signature. KKAYVTLKegqnldfV
ChainResidueDetails
TLYS81-VAL96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues35
DetailsTransmembrane: {"description":"Discontinuously helical; Name=2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsIntramembrane: {"description":"Helical; Name=Helix 2A","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsIntramembrane: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues19
DetailsIntramembrane: {"description":"Helical; Name=Helix 2B","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues107
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues80
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues13
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues13
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues13
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues14
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues43
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues24
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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