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

2YXQ

The plug domain of the SecY protein stablizes the closed state of the translocation channel and maintains a membrane seal

Functional Information from GO Data
ChainGOidnamespacecontents
A0005048molecular_functionsignal sequence binding
A0005886cellular_componentplasma membrane
A0006605biological_processprotein targeting
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
A0043022molecular_functionribosome binding
A0065002biological_processintracellular protein transmembrane transport
B0005886cellular_componentplasma membrane
B0006605biological_processprotein targeting
B0006886biological_processintracellular protein transport
B0008320molecular_functionprotein transmembrane transporter activity
B0009306biological_processprotein secretion
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0065002biological_processintracellular protein transmembrane transport
C0005886cellular_componentplasma membrane
C0015031biological_processprotein transport
C0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00318
Number of Residues8
DetailsHMG_COA_REDUCTASE_2 Hydroxymethylglutaryl-coenzyme A reductases signature 2. IGaLGGGT
ChainResidueDetails
AILE395-THR402

site_idPS00755
Number of Residues20
DetailsSECY_1 Protein secY signature 1. TLItLGIgPIVtAGIIMQLL
ChainResidueDetails
ATHR69-LEU88

site_idPS00756
Number of Residues18
DetailsSECY_2 Protein secY signature 2. YLdEiVSky.GIGSGiGLF
ChainResidueDetails
ATYR156-PHE173

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues29
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
CMET1-PRO30
AILE94-SER115
AGLY167-PHE173
AILE233-ILE260
ATHR337-PHE387

site_idSWS_FT_FI2
Number of Residues18
DetailsTRANSMEM: Helical
ChainResidueDetails
CGLU31-TYR49

site_idSWS_FT_FI3
Number of Residues3
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
CGLY50-LEU53
ALEU135-ILE145
ALEU197-ILE214
AILE283-ILE317
AGLY403

site_idSWS_FT_FI4
Number of Residues32
DetailsTRANSMEM: Discontinuously helical; Name=Helix 2
ChainResidueDetails
APHE56-ILE93

site_idSWS_FT_FI5
Number of Residues7
DetailsINTRAMEM: Helical; Name=Helix 2A
ChainResidueDetails
APHE56-GLY68

site_idSWS_FT_FI6
Number of Residues5
DetailsINTRAMEM:
ChainResidueDetails
ATHR69-GLY74

site_idSWS_FT_FI7
Number of Residues18
DetailsINTRAMEM: Helical; Name=Helix 2B
ChainResidueDetails
AILE75-ILE93

site_idSWS_FT_FI8
Number of Residues18
DetailsTRANSMEM: Helical; Name=Helix 3
ChainResidueDetails
AILE116-ILE134

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=Helix 4
ChainResidueDetails
AGLN146-ILE166

site_idSWS_FT_FI10
Number of Residues22
DetailsTRANSMEM: Helical; Name=Helix 5
ChainResidueDetails
AILE174-PHE196

site_idSWS_FT_FI11
Number of Residues17
DetailsTRANSMEM: Helical; Name=Helix 6
ChainResidueDetails
AGLY215-GLU232

site_idSWS_FT_FI12
Number of Residues21
DetailsTRANSMEM: Helical; Name=Helix 7
ChainResidueDetails
ALEU261-PRO282

site_idSWS_FT_FI13
Number of Residues18
DetailsTRANSMEM: Helical; Name=Helix 8
ChainResidueDetails
AVAL318-GLU336

site_idSWS_FT_FI14
Number of Residues14
DetailsTRANSMEM: Helical; Name=Helix 9
ChainResidueDetails
ALEU388-THR402

site_idSWS_FT_FI15
Number of Residues13
DetailsTRANSMEM: Helical; Name=Helix 10
ChainResidueDetails
AVAL404-GLN417

site_idSWS_FT_FI16
Number of Residues6
DetailsSITE: Pore ring
ChainResidueDetails
ATHR80
AILE84
ASER179
AVAL184
ALEU265
AVAL411

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon