6AJG
Crystal structure of mycolic acid transporter MmpL3 from Mycobacterium smegmatis complexed with SQ109
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme activity |
A | 0003824 | molecular_function | catalytic activity |
A | 0009253 | biological_process | peptidoglycan catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
A | 0030430 | cellular_component | host cell cytoplasm |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0042742 | biological_process | defense response to bacterium |
A | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue 3RX A 1001 |
Chain | Residue |
A | ILE249 |
A | ASP645 |
A | ILE253 |
A | ASP256 |
A | TYR257 |
A | ILE297 |
A | SER301 |
A | ALA637 |
A | VAL638 |
A | LEU642 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue LMT A 1002 |
Chain | Residue |
A | THR66 |
A | SER67 |
A | VAL109 |
A | ASP119 |
A | THR121 |
A | SER136 |
A | LEU171 |
A | LEU174 |
A | GLN442 |
A | ARG453 |
A | LMT1003 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue LMT A 1003 |
Chain | Residue |
A | GLN40 |
A | ASP64 |
A | SER67 |
A | ILE182 |
A | HIS239 |
A | PHE240 |
A | PHE241 |
A | ILE427 |
A | ARG453 |
A | THR454 |
A | GLU455 |
A | THR549 |
A | LEU698 |
A | LMT1002 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue LMT A 1004 |
Chain | Residue |
A | LEU422 |
A | SER423 |
A | LEU424 |
A | GLN554 |
A | ILE557 |
A | LEU564 |
A | LEU600 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue LMT A 1005 |
Chain | Residue |
A | LEU23 |
A | GLY27 |
A | TYR30 |
A | ASP77 |
A | LYS79 |
A | GLU234 |
A | PHE235 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue LMT A 1006 |
Chain | Residue |
A | LEU25 |
A | ILE32 |
A | GLY35 |
A | THR179 |
A | GLY180 |
A | ILE182 |
A | GLY183 |
A | LEU226 |
A | PHE240 |
A | GLN243 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue LMT A 1007 |
Chain | Residue |
A | GLN-3 |
A | THR285 |
A | ARG288 |
A | THR289 |
A | PHE292 |
A | LEU581 |
A | ALA582 |
A | SER652 |
A | ARG653 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue LMT A 1008 |
Chain | Residue |
A | TRP390 |
A | THR672 |
A | ALA673 |
A | GLY676 |
A | THR680 |
A | ARG720 |
A | MET721 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue LMT A 1009 |
Chain | Residue |
A | THR236 |
A | LYS313 |
A | TYR317 |
A | LMT1010 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue LMT A 1010 |
Chain | Residue |
A | TYR317 |
A | LMT1009 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue MHA A 1011 |
Chain | Residue |
A | ASP759 |
A | THR891 |
A | PRO892 |
A | ASN893 |
A | ARG894 |
A | ILE917 |
A | LYS918 |
A | ALA919 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue MHA A 1012 |
Chain | Residue |
A | GLY618 |
A | GLY862 |
A | PHE863 |
A | THR864 |
A | ASN865 |
A | SER866 |
A | ASN881 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 69 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 240 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 330 |
Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 28 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 19 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6OR2","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6AJG","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | Site: {"description":"Part of the proton-transportation channel","evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Site: {"description":"Part of the proton transportation network","evidences":[{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Site: {"description":"Part of the proton-transportation channel","evidences":[{"source":"PubMed","id":"30682372","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31113875","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32512002","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |