6FMS
IMISX-EP of Se-LspA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004175 | molecular_function | endopeptidase activity |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006465 | biological_process | signal peptide processing |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004175 | molecular_function | endopeptidase activity |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006465 | biological_process | signal peptide processing |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0004175 | molecular_function | endopeptidase activity |
| C | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006465 | biological_process | signal peptide processing |
| C | 0006508 | biological_process | proteolysis |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0004175 | molecular_function | endopeptidase activity |
| D | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006465 | biological_process | signal peptide processing |
| D | 0006508 | biological_process | proteolysis |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0016020 | cellular_component | membrane |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 201 |
| Chain | Residue |
| A | PHE29 |
| A | ILE40 |
| A | OLC202 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 202 |
| Chain | Residue |
| A | VAL42 |
| A | TRP49 |
| A | OLC201 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 203 |
| Chain | Residue |
| D | ALA28 |
| D | ALA32 |
| E | OLC301 |
| A | PRO11 |
| A | TRP12 |
| A | ILE15 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 204 |
| Chain | Residue |
| A | PHE7 |
| A | LEU10 |
| A | PRO11 |
| A | TRP14 |
| D | GLN31 |
| D | TYR114 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 205 |
| Chain | Residue |
| A | ARG70 |
| A | MSE117 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue OLC B 202 |
| Chain | Residue |
| B | GLY8 |
| B | ARG9 |
| B | PRO11 |
| B | TRP12 |
| B | ILE15 |
| B | LYS93 |
| B | LEU104 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC B 203 |
| Chain | Residue |
| B | LEU10 |
| B | TRP14 |
| C | TYR114 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue OLC B 204 |
| Chain | Residue |
| A | ALA63 |
| A | ASP64 |
| B | TRP130 |
| B | ARG133 |
| B | TRP134 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue OLC B 205 |
| Chain | Residue |
| B | GLU33 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue OLC B 206 |
| Chain | Residue |
| B | TRP49 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue OLC C 201 |
| Chain | Residue |
| C | PHE139 |
| C | ASP143 |
| C | THR147 |
| G | IIL202 |
| G | ALO204 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue OLC C 202 |
| Chain | Residue |
| C | VAL41 |
| C | TRP49 |
| C | OLC205 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue OLC C 203 |
| Chain | Residue |
| C | LEU110 |
| C | MSE117 |
| C | VAL118 |
| C | OLC204 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue OLC C 204 |
| Chain | Residue |
| C | ARG70 |
| C | MSE117 |
| C | OLC203 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue OLC C 205 |
| Chain | Residue |
| C | PHE29 |
| C | GLU33 |
| C | TRP49 |
| C | OLC202 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC D 201 |
| Chain | Residue |
| D | PHE29 |
| D | ILE40 |
| D | OLC202 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue OLC D 202 |
| Chain | Residue |
| D | TRP49 |
| D | OLC201 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue OLC E 301 |
| Chain | Residue |
| A | PHE139 |
| A | ASP143 |
| A | VAL148 |
| A | OLC203 |
| E | IIL202 |
| E | SER203 |
| E | ALO204 |
| site_id | AE1 |
| Number of Residues | 8 |
| Details | binding site for residue OLC F 301 |
| Chain | Residue |
| B | THR55 |
| B | PRO137 |
| B | PHE139 |
| B | ASP143 |
| B | THR147 |
| F | IIL202 |
| F | SER203 |
| F | ALO204 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue OLC H 301 |
| Chain | Residue |
| D | PHE139 |
| D | ASP143 |
| D | THR147 |
| H | IIL202 |
| H | SER203 |
| H | ALO204 |
| site_id | AE3 |
| Number of Residues | 9 |
| Details | binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203 |
| Chain | Residue |
| A | ASN54 |
| A | GLY56 |
| A | PHE59 |
| A | PHE73 |
| A | ASN112 |
| A | ARG116 |
| A | ASP124 |
| A | ASP143 |
| E | OLC301 |
| site_id | AE4 |
| Number of Residues | 12 |
| Details | binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203 |
| Chain | Residue |
| B | ASN140 |
| B | ASP143 |
| B | ILE146 |
| F | OLC301 |
| B | LEU62 |
| B | PHE73 |
| B | ALA77 |
| B | VAL80 |
| B | ASN112 |
| B | ARG116 |
| B | VAL122 |
| B | ASP124 |
| site_id | AE5 |
| Number of Residues | 12 |
| Details | binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203 |
| Chain | Residue |
| C | ASN54 |
| C | PHE59 |
| C | PHE73 |
| C | ALA77 |
| C | ASN112 |
| C | ARG116 |
| C | VAL122 |
| C | ASP124 |
| C | ASP143 |
| C | ILE146 |
| C | OLC201 |
| H | 5BV205 |
| site_id | AE6 |
| Number of Residues | 13 |
| Details | binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203 |
| Chain | Residue |
| D | ASN54 |
| D | ALA57 |
| D | PHE59 |
| D | PHE73 |
| D | VAL80 |
| D | ALA109 |
| D | ASN112 |
| D | ARG116 |
| D | ASP124 |
| D | ASP143 |
| D | ILE146 |
| G | 5BV205 |
| H | OLC301 |
Functional Information from PROSITE/UniProt
| site_id | PS00855 |
| Number of Residues | 13 |
| Details | SPASE_II Signal peptidases II signature. VlGGALGNLYDRM |
| Chain | Residue | Details |
| A | VAL105-MSE117 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00161","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30272004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FMS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 84 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30272004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FMS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30272004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FMS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 84 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30272004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DIR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FMS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00161","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26912896","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
