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3DIN

Crystal structure of the protein-translocation complex formed by the SecY channel and the SecA ATPase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006605biological_processprotein targeting
A0006886biological_processintracellular protein transport
A0008564molecular_functionprotein-exporting ATPase activity
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0017038biological_processprotein import
A0031522cellular_componentcell envelope Sec protein transport complex
A0043952biological_processprotein transport by the Sec complex
A0065002biological_processintracellular protein transmembrane transport
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006605biological_processprotein targeting
B0006886biological_processintracellular protein transport
B0008564molecular_functionprotein-exporting ATPase activity
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0017038biological_processprotein import
B0031522cellular_componentcell envelope Sec protein transport complex
B0043952biological_processprotein transport by the Sec complex
B0065002biological_processintracellular protein transmembrane transport
C0005048molecular_functionsignal sequence binding
C0005886cellular_componentplasma membrane
C0006605biological_processprotein targeting
C0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
C0008320molecular_functionprotein transmembrane transporter activity
C0015031biological_processprotein transport
C0016020cellular_componentmembrane
C0031522cellular_componentcell envelope Sec protein transport complex
C0043952biological_processprotein transport by the Sec complex
C0065002biological_processintracellular protein transmembrane transport
D0005886cellular_componentplasma membrane
D0006605biological_processprotein targeting
D0006886biological_processintracellular protein transport
D0008320molecular_functionprotein transmembrane transporter activity
D0009306biological_processprotein secretion
D0015031biological_processprotein transport
D0016020cellular_componentmembrane
D0043952biological_processprotein transport by the Sec complex
D0065002biological_processintracellular protein transmembrane transport
E0009306biological_processprotein secretion
E0015450molecular_functionprotein-transporting ATPase activity
E0016020cellular_componentmembrane
F0005048molecular_functionsignal sequence binding
F0005886cellular_componentplasma membrane
F0006605biological_processprotein targeting
F0006616biological_processSRP-dependent cotranslational protein targeting to membrane, translocation
F0008320molecular_functionprotein transmembrane transporter activity
F0015031biological_processprotein transport
F0016020cellular_componentmembrane
F0031522cellular_componentcell envelope Sec protein transport complex
F0043952biological_processprotein transport by the Sec complex
F0065002biological_processintracellular protein transmembrane transport
G0005886cellular_componentplasma membrane
G0006605biological_processprotein targeting
G0006886biological_processintracellular protein transport
G0008320molecular_functionprotein transmembrane transporter activity
G0009306biological_processprotein secretion
G0015031biological_processprotein transport
G0016020cellular_componentmembrane
G0043952biological_processprotein transport by the Sec complex
G0065002biological_processintracellular protein transmembrane transport
H0009306biological_processprotein secretion
H0015450molecular_functionprotein-transporting ATPase activity
H0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 872
ChainResidue
ALYS101
ATHR102
AARG131
AASP252

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 872
ChainResidue
BLYS101
BTHR102
BARG131
BASP252

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADP A 873
ChainResidue
AARG75
APRO76
ALYS96
ATHR97
AGLY98
AGLY100
ALYS101
ATHR102
ALEU103
ATRP135
ALEU187
AASP537
AARG573
AGLN574
AMET74

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEF A 874
ChainResidue
ALYS101
AARG131
AASP252
AGLU253
AGLY535
ATHR536

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADP B 873
ChainResidue
BMET74
BARG75
BPRO76
BLYS96
BTHR97
BGLY98
BGLY100
BLYS101
BTHR102
BLEU103
BTRP135
BLEU187
BASP537
BARG573
BGLN574

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEF B 874
ChainResidue
BLYS101
BARG131
BASP252
BGLU253
BGLY535
BTHR536

Functional Information from PROSITE/UniProt
site_idPS00755
Number of Residues20
DetailsSECY_1 Protein secY signature 1. SVFtMSVtPYItASIILQLL
ChainResidueDetails
CSER76-LEU95

site_idPS00756
Number of Residues18
DetailsSECY_2 Protein secY signature 2. WLgErITek.GIGNGiSIL
ChainResidueDetails
CTRP173-LEU190

site_idPS01067
Number of Residues29
DetailsSECE_SEC61G Protein secE/sec61-gamma signature. FfREvIaeAkKisWPsrkElltsfGVVLV
ChainResidueDetails
DPHE7-VAL35

site_idPS01312
Number of Residues16
DetailsSECA SecA family signature. VtIATNMAGRGtDIkL
ChainResidueDetails
AVAL525-LEU540

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01382","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=Helix 1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues42
DetailsTransmembrane: {"description":"Discontinuously helical; Name=Helix 2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsIntramembrane: {"description":"Helical; Name=Helix 2A"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsIntramembrane: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsIntramembrane: {"description":"Helical; Name=Helix 2B"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues242
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=Helix 3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues130
DetailsTopological domain: {"description":"Periplasmic"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues32
DetailsTransmembrane: {"description":"Helical; Name=Helix 4"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues30
DetailsTransmembrane: {"description":"Helical; Name=Helix 5"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=Helix 6"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=Helix 7"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=Helix 8"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=Helix 9"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=Helix 10"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues32
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues26
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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