4FW3
Crystal Structure of the LpxC in complex with N-[(2S)-3-AMINO-1-(HYDROXYAMINO)-1-OXOPROPAN-2-YL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE 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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | HIS78 |
| A | HIS237 |
| A | ASP241 |
| A | L52302 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE L52 A 302 |
| Chain | Residue |
| A | PHE191 |
| A | GLY209 |
| A | SER210 |
| A | HIS237 |
| A | ASP241 |
| A | HIS264 |
| A | ZN301 |
| A | HOH464 |
| A | HIS19 |
| A | MET62 |
| A | GLU77 |
| A | HIS78 |
| A | THR190 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | ALA84 |
| A | PHE152 |
| A | ILE243 |
| A | LEU246 |
| A | TYR247 |
| A | SER252 |
| A | LEU253 |
| A | HOH466 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 300 |
| Chain | Residue |
| B | HIS78 |
| B | HIS237 |
| B | ASP241 |
| B | L52301 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE L52 B 301 |
| Chain | Residue |
| B | GLU77 |
| B | HIS78 |
| B | THR190 |
| B | PHE191 |
| B | ILE197 |
| B | ARG201 |
| B | GLY209 |
| B | SER210 |
| B | VAL216 |
| B | HIS237 |
| B | ASP241 |
| B | HIS264 |
| B | ZN300 |
| B | HOH473 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 300 |
| Chain | Residue |
| C | HIS78 |
| C | HIS237 |
| C | ASP241 |
| C | L52301 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE L52 C 301 |
| Chain | Residue |
| C | MET62 |
| C | GLU77 |
| C | HIS78 |
| C | THR190 |
| C | PHE191 |
| C | ILE197 |
| C | GLY209 |
| C | SER210 |
| C | VAL216 |
| C | HIS237 |
| C | ASP241 |
| C | HIS264 |
| C | ZN300 |
| C | HOH469 |
| C | HOH482 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | HIS78 |
| D | HIS237 |
| D | ASP241 |
| D | L52302 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE L52 D 302 |
| Chain | Residue |
| D | LEU18 |
| D | HIS19 |
| D | MET62 |
| D | GLU77 |
| D | HIS78 |
| D | THR190 |
| D | MET194 |
| D | ARG201 |
| D | SER210 |
| D | HIS237 |
| D | ASP241 |
| D | HIS264 |
| D | ZN301 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 303 |
| Chain | Residue |
| D | ALA84 |
| D | PHE152 |
| D | ILE243 |
| D | LEU246 |
| D | TYR247 |
| D | SER252 |
| D | LEU253 |
| D | HOH418 |
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 |
