7CI5
Crystal structure of P.aeruginosa LpxC in complex with inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0009245 | biological_process | lipid A biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0009245 | biological_process | lipid A biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue FXX A 301 |
| Chain | Residue |
| A | LEU18 |
| A | LYS238 |
| A | ASP241 |
| A | HIS264 |
| A | ZN303 |
| A | HOH415 |
| A | MET62 |
| A | GLU77 |
| A | HIS78 |
| A | ILE197 |
| A | GLY209 |
| A | ASN213 |
| A | ALA214 |
| A | HIS237 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MPO A 302 |
| Chain | Residue |
| A | ARG41 |
| A | ASP70 |
| A | LYS72 |
| A | SER98 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 303 |
| Chain | Residue |
| A | HIS78 |
| A | HIS237 |
| A | ASP241 |
| A | FXX301 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue FXX B 301 |
| Chain | Residue |
| B | LEU18 |
| B | MET62 |
| B | GLU77 |
| B | HIS78 |
| B | ILE102 |
| B | ILE197 |
| B | GLY209 |
| B | ASN213 |
| B | ALA214 |
| B | HIS237 |
| B | LYS238 |
| B | ASP241 |
| B | HIS264 |
| B | ZN303 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MPO B 302 |
| Chain | Residue |
| B | ARG41 |
| B | ASP70 |
| B | LYS72 |
| B | SER98 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 303 |
| Chain | Residue |
| B | HIS78 |
| B | HIS237 |
| B | ASP241 |
| B | FXX301 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue FXX C 301 |
| Chain | Residue |
| C | LEU18 |
| C | MET62 |
| C | GLU77 |
| C | HIS78 |
| C | ILE197 |
| C | ASN213 |
| C | ALA214 |
| C | HIS237 |
| C | LYS238 |
| C | ASP241 |
| C | HIS264 |
| C | ZN303 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MPO C 302 |
| Chain | Residue |
| C | ARG41 |
| C | ASP70 |
| C | VAL71 |
| C | LYS72 |
| C | SER98 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 303 |
| Chain | Residue |
| C | HIS78 |
| C | HIS237 |
| C | ASP241 |
| C | FXX301 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue FXX D 301 |
| Chain | Residue |
| D | LEU18 |
| D | MET62 |
| D | GLU77 |
| D | HIS78 |
| D | THR190 |
| D | ILE197 |
| D | GLY209 |
| D | ASN213 |
| D | HIS237 |
| D | LYS238 |
| D | ASP241 |
| D | HIS264 |
| D | ZN303 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MPO D 302 |
| Chain | Residue |
| D | ARG41 |
| D | ASP70 |
| D | VAL71 |
| D | LYS72 |
| D | SER98 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 303 |
| Chain | Residue |
| D | HIS78 |
| D | HIS237 |
| D | ASP241 |
| D | FXX301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
