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

1M74

Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 902
ChainResidue
ATHR107
AASP207
AADP901
AHOH1146
AHOH1147

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AHOH1101
ATHR58
ATHR120
ALYS122
AHIS202

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
AASN130
AGLU131
AHIS464

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1005
ChainResidue
ALEU596
AARG735
AGLN736

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1006
ChainResidue
ATYR408
AARG409
ATHR410
ATHR567

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1007
ChainResidue
AGLU216
AARG218
ATHR219
AGLN798
APRO799

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ADP A 901
ChainResidue
AMET79
APHE80
APRO81
APHE82
AGLN85
AGLY103
AGLU104
AGLY105
ALYS106
ATHR107
ALEU108
AGLY490
AASP492
AARG528
AMG902
AHOH1146
AHOH1147

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 Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:19850053, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:3JV2
ChainResidueDetails
AMET79

site_idSWS_FT_FI2
Number of Residues2
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

site_idSWS_FT_FI3
Number of Residues1
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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon