Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9EMZ

13C/15N-labelled Integral Membrane Enzyme LspA in the Lipid Cubic Phase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004190molecular_functionaspartic-type endopeptidase activity
A0005886cellular_componentplasma membrane
A0006465biological_processsignal peptide processing
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
B0004175molecular_functionendopeptidase activity
B0004190molecular_functionaspartic-type endopeptidase activity
B0005886cellular_componentplasma membrane
B0006465biological_processsignal peptide processing
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
C0004175molecular_functionendopeptidase activity
C0004190molecular_functionaspartic-type endopeptidase activity
C0005886cellular_componentplasma membrane
C0006465biological_processsignal peptide processing
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
D0004175molecular_functionendopeptidase activity
D0004190molecular_functionaspartic-type endopeptidase activity
D0005886cellular_componentplasma membrane
D0006465biological_processsignal peptide processing
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00855
Number of Residues13
DetailsSPASE_II Signal peptidases II signature. VlGGALGNLYDRM
ChainResidueDetails
AVAL105-MET117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
ChainResidueDetails
AMET1-ARG9
AARG90-THR96
BMET1-ARG9
BARG90-THR96
CMET1-ARG9
CARG90-THR96
DMET1-ARG9
DARG90-THR96

site_idSWS_FT_FI2
Number of Residues80
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
ChainResidueDetails
ALEU10-PHE30
BLEU10-PHE30
CLEU10-PHE30
DLEU10-PHE30

site_idSWS_FT_FI3
Number of Residues228
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
ChainResidueDetails
AGLN31-GLY67
ALEU119-ASN140
BGLN31-GLY67
BLEU119-ASN140
CGLN31-GLY67
CLEU119-ASN140
DGLN31-GLY67
DLEU119-ASN140

site_idSWS_FT_FI4
Number of Residues168
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26912896, ECO:0000269|PubMed:30272004, ECO:0007744|PDB:5DIR, ECO:0007744|PDB:6FMS
ChainResidueDetails
ATRP68-LYS89
ATRP97-VAL118
BTRP68-LYS89
BTRP97-VAL118
CTRP68-LYS89
CTRP97-VAL118
DTRP68-LYS89
DTRP97-VAL118

site_idSWS_FT_FI5
Number of Residues52
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26912896, ECO:0007744|PDB:5DIR
ChainResidueDetails
ALEU141-ALA154
BLEU141-ALA154
CLEU141-ALA154
DLEU141-ALA154

site_idSWS_FT_FI6
Number of Residues56
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26912896, ECO:0007744|PDB:5DIR
ChainResidueDetails
ALEU155-GLY169
BLEU155-GLY169
CLEU155-GLY169
DLEU155-GLY169

site_idSWS_FT_FI7
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000305|PubMed:26912896
ChainResidueDetails
AASP124
AASP143
BASP124
BASP143
CASP124
CASP143
DASP124
DASP143

237992

PDB entries from 2025-06-25

PDB statisticsPDBj update infoContact PDBjnumon