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3JV2

Crystal Structure of B. subtilis SecA with bound peptide

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0045121cellular_componentmembrane raft
A0046872molecular_functionmetal ion binding
A0065002biological_processintracellular protein transmembrane transport
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
B0045121cellular_componentmembrane raft
B0046872molecular_functionmetal ion binding
B0065002biological_processintracellular protein transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 872
ChainResidue
ATHR107
AASP207
AHOH810
AHOH859
AHOH860
AHOH861
AADP873

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A 873
ChainResidue
APRO81
APHE82
AGLN85
ATHR102
AGLY103
AGLU104
AGLY105
ALYS106
ATHR107
ALEU108
ALYS494
AHOH859
AHOH860
AMG872
AMET79
APHE80

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 872
ChainResidue
BTHR107
BASP207
BHOH794
BHOH800
BHOH850
BHOH851
BADP873

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP B 873
ChainResidue
BMET79
BPHE80
BPRO81
BPHE82
BGLN85
BTHR102
BGLY103
BGLU104
BGLY105
BLYS106
BTHR107
BHOH850
BHOH851
BMG872

Functional Information from PROSITE/UniProt
site_idPS01312
Number of Residues16
DetailsSECA SecA family signature. VtIATNMAGRGtDIkL
ChainResidueDetails
AVAL480-LEU495

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:19850053, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:3JV2
ChainResidueDetails
AMET79
BMET79

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:16989859, ECO:0000269|PubMed:19850053, ECO:0007744|PDB:1M74, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:2IBM, ECO:0007744|PDB:3JV2
ChainResidueDetails
AGLN85
AGLY103
BGLN85
BGLY103

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:16989859, ECO:0007744|PDB:1M74, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:2IBM
ChainResidueDetails
AASP492
BASP492

220113

PDB entries from 2024-05-22

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