Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8DNZ

Cryo-EM structure of the human Sec61 complex inhibited by apratoxin F

Functional Information from GO Data
ChainGOidnamespacecontents
A0005048molecular_functionsignal sequence binding
A0005262molecular_functioncalcium channel activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005784cellular_componentSec61 translocon complex
A0005789cellular_componentendoplasmic reticulum membrane
A0006613biological_processcotranslational protein targeting to membrane
A0006614biological_processSRP-dependent cotranslational protein targeting to membrane
A0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
A0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
A0007029biological_processendoplasmic reticulum organization
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
A0070588biological_processcalcium ion transmembrane transport
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0006605biological_processprotein targeting
B0006886biological_processintracellular protein transport
B0008320molecular_functionprotein transmembrane transporter activity
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0031204biological_processpost-translational protein targeting to membrane, translocation
B0043022molecular_functionribosome binding
B0045047biological_processprotein targeting to ER
B0071261cellular_componentSsh1 translocon complex
C0003723molecular_functionRNA binding
C0005085molecular_functionguanyl-nucleotide exchange factor activity
C0005515molecular_functionprotein binding
C0005783cellular_componentendoplasmic reticulum
C0005784cellular_componentSec61 translocon complex
C0005789cellular_componentendoplasmic reticulum membrane
C0005829cellular_componentcytosol
C0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
C0006886biological_processintracellular protein transport
C0015031biological_processprotein transport
C0016020cellular_componentmembrane
C0030970biological_processretrograde protein transport, ER to cytosol
C0031204biological_processpost-translational protein targeting to membrane, translocation
C0031205cellular_componentendoplasmic reticulum Sec complex
C0036503biological_processERAD pathway
C0043022molecular_functionribosome binding
C0044322cellular_componentendoplasmic reticulum quality control compartment
C0048408molecular_functionepidermal growth factor binding
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 Residues141
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-LEU33
AALA97-LYS117
AASP166-GLY172
AARG262-ASN288
ASER376-ALA420
ALYS463-PHE476

site_idSWS_FT_FI2
Number of Residues194
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ATRP34-ILE53
AMET77-GLY96
ALEU118-GLY138
AALA145-LEU165
ATYR173-TRP193
AASN241-PHE261
AILE289-SER309
ALEU355-PHE375
AALA421-ILE441
AGLY446-VAL462

site_idSWS_FT_FI3
Number of Residues120
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
AMET54-LEU76
AASP139-GLY144
ALYS194-PRO240
AALA310-VAL354
AGLY442-THR445

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylproline => ECO:0007744|PubMed:21406692
ChainResidueDetails
CPRO2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|Ref.5
ChainResidueDetails
CSER7

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR9

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
CSER13

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER14

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CSER17

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000305|PubMed:21044946
ChainResidueDetails
CCYS39

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon