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4CG7

Cryo-EM of the Sec61-complex bound to the idle 80S ribosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0005048molecular_functionsignal sequence binding
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005784cellular_componentSec61 translocon complex
A0005789cellular_componentendoplasmic reticulum membrane
A0006613biological_processcotranslational protein targeting to membrane
A0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
A0008320molecular_functionprotein transmembrane 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
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006605biological_processprotein targeting
B0006886biological_processintracellular protein transport
B0008320molecular_functionprotein transmembrane 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
C0005784cellular_componentSec61 translocon complex
C0006886biological_processintracellular protein transport
Functional Information from PROSITE/UniProt
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_idPS01067
Number of Residues29
DetailsSECE_SEC61G Protein secE/sec61-gamma signature. FvKDsIrlVkRctKPdrkEfqkiaMATAI
ChainResidueDetails
BPHE14-ILE42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues19
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT
ChainResidueDetails
CPRO72-GLY91
ALYS98-ARG109
ALEU168-SER177
AGLY260-TYR285
AILE380-ALA420
AGLU459-PHE476

site_idSWS_FT_FI2
Number of Residues4
DetailsTOPO_DOM: Lumenal => ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT
ChainResidueDetails
CLYS92-SER96
AGLY444-PHE458
AILE81-ALA97
AALA110-TYR131
ALEU149-GLU167
AGLY178-PHE196
ALEU242-GLN259
ATHR286-GLN306
AASP357-TRP379
AALA421-PHE437

site_idSWS_FT_FI3
Number of Residues6
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:36261528, ECO:0007744|PDB:7TM3, ECO:0007744|PDB:7TUT
ChainResidueDetails
BASN62-GLY68
AVAL132-CYS148
ASER197-ASN241
AMET307-GLU356
ALEU438-SER443

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P60059
ChainResidueDetails
BMET1

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60059
ChainResidueDetails
BSER18

226707

PDB entries from 2024-10-30

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