4FW6
Crystal Structure of the LpxC in complex with N-[(2S,3R)-3-HYDROXY-1-(HYDROXYAMINO)-1-OXOBUTAN-2-YL]-4-(PHENYLETHYNYL)BENZAMIDE inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019637 | biological_process | organophosphate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| B | 0006796 | biological_process | phosphate-containing compound metabolic process |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019637 | biological_process | organophosphate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| B | 1901135 | biological_process | carbohydrate derivative metabolic process |
| C | 0006796 | biological_process | phosphate-containing compound metabolic process |
| C | 0009245 | biological_process | lipid A biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019637 | biological_process | organophosphate metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| C | 1901135 | biological_process | carbohydrate derivative metabolic process |
| D | 0006796 | biological_process | phosphate-containing compound metabolic process |
| D | 0009245 | biological_process | lipid A biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019637 | biological_process | organophosphate metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0103117 | molecular_function | UDP-3-O-acyl-N-acetylglucosamine deacetylase activity |
| D | 1901135 | biological_process | carbohydrate derivative metabolic process |
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 | L59302 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE L59 A 302 |
| Chain | Residue |
| A | LEU200 |
| A | ARG201 |
| A | GLY209 |
| A | SER210 |
| A | VAL216 |
| A | HIS237 |
| A | ASP241 |
| A | HIS264 |
| A | ZN301 |
| A | PEG308 |
| A | HOH449 |
| A | GLU77 |
| A | HIS78 |
| A | THR190 |
| A | PHE191 |
| A | ILE197 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | ILE243 |
| A | LEU246 |
| A | TYR247 |
| A | ASN251 |
| A | SER252 |
| A | LEU253 |
| A | HOH440 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 304 |
| Chain | Residue |
| A | PHE149 |
| A | HOH430 |
| A | HOH436 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 305 |
| Chain | Residue |
| A | ARG143 |
| A | ARG258 |
| A | GLY259 |
| A | PHE260 |
| A | HOH498 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 306 |
| Chain | Residue |
| A | GLU139 |
| A | GLY140 |
| A | ASP141 |
| A | ASP226 |
| C | ASN-1 |
| C | ALA0 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 307 |
| Chain | Residue |
| A | GLU139 |
| A | ARG189 |
| A | ARG229 |
| A | GLN269 |
| A | HOH475 |
| A | HOH551 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 308 |
| Chain | Residue |
| A | MET194 |
| A | SER210 |
| A | VAL211 |
| A | L59302 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 309 |
| Chain | Residue |
| A | ARG53 |
| A | GLU55 |
| A | SER116 |
| A | LEU249 |
| A | ILE275 |
| A | HOH443 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HIS78 |
| B | HIS237 |
| B | ASP241 |
| B | L59302 |
| site_id | BC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE L59 B 302 |
| Chain | Residue |
| B | MET62 |
| B | GLU77 |
| B | HIS78 |
| B | THR190 |
| B | PHE191 |
| B | ILE197 |
| B | LEU200 |
| B | ARG201 |
| B | GLY209 |
| B | SER210 |
| B | VAL216 |
| B | HIS237 |
| B | ASP241 |
| B | HIS264 |
| B | ZN301 |
| B | HOH533 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| B | PHE152 |
| B | ILE243 |
| B | LEU246 |
| B | TYR247 |
| B | SER252 |
| B | LEU253 |
| B | HOH556 |
| B | HOH576 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 304 |
| Chain | Residue |
| B | HOH443 |
| B | HOH461 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 305 |
| Chain | Residue |
| B | GLU139 |
| B | GLY140 |
| B | ASP141 |
| B | ASP226 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 306 |
| Chain | Residue |
| B | ARG143 |
| B | VAL145 |
| B | ARG258 |
| B | GLY259 |
| B | PHE260 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 307 |
| Chain | Residue |
| B | THR285 |
| D | LEU207 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 308 |
| Chain | Residue |
| B | HOH425 |
| B | HOH594 |
| B | VAL211 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B 309 |
| Chain | Residue |
| B | GLY108 |
| B | PRO109 |
| B | VAL111 |
| B | SER186 |
| B | ARG272 |
| B | THR273 |
| B | HOH473 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 301 |
| Chain | Residue |
| C | HIS78 |
| C | HIS237 |
| C | ASP241 |
| C | L59302 |
| site_id | CC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE L59 C 302 |
| Chain | Residue |
| C | MET62 |
| C | GLU77 |
| C | HIS78 |
| C | THR190 |
| C | PHE191 |
| C | ILE197 |
| C | GLY209 |
| C | SER210 |
| C | VAL216 |
| C | HIS237 |
| C | LYS238 |
| C | ASP241 |
| C | HIS264 |
| C | ZN301 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 303 |
| Chain | Residue |
| C | ILE243 |
| C | LEU246 |
| C | TYR247 |
| C | ASN251 |
| C | SER252 |
| C | LEU253 |
| C | HOH502 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 304 |
| Chain | Residue |
| C | ASP104 |
| C | GLY108 |
| C | PRO109 |
| C | VAL111 |
| C | PHE112 |
| C | ARG187 |
| C | ARG272 |
| C | THR273 |
| C | HOH445 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 305 |
| Chain | Residue |
| C | ARG53 |
| C | ILE129 |
| C | LEU249 |
| C | ASN251 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 306 |
| Chain | Residue |
| C | GLU59 |
| C | SER63 |
| C | ASP74 |
| C | HOH523 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 307 |
| Chain | Residue |
| C | GLY140 |
| C | LEU228 |
| C | GLU231 |
| C | HOH535 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | HIS78 |
| D | HIS237 |
| D | ASP241 |
| D | L59302 |
| site_id | CC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE L59 D 302 |
| Chain | Residue |
| D | MET62 |
| D | GLU77 |
| D | HIS78 |
| D | THR190 |
| D | PHE191 |
| D | ILE197 |
| D | ARG201 |
| D | GLY209 |
| D | SER210 |
| D | VAL216 |
| D | HIS237 |
| D | LYS238 |
| D | ASP241 |
| D | HIS264 |
| D | ZN301 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 303 |
| Chain | Residue |
| D | PHE152 |
| D | ILE243 |
| D | LEU246 |
| D | TYR247 |
| D | SER252 |
| D | LEU253 |
| D | HOH517 |
| site_id | DC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 304 |
| Chain | Residue |
| D | ASP104 |
| D | GLY108 |
| D | PRO109 |
| D | VAL111 |
| D | PHE112 |
| D | ARG187 |
| D | ARG272 |
| D | THR273 |
| D | HOH440 |
| site_id | DC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 305 |
| Chain | Residue |
| D | ALA31 |
| D | GLN122 |
| D | HOH439 |
| site_id | DC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 306 |
| Chain | Residue |
| D | SER40 |
| D | GLU49 |
| D | GLU94 |
| site_id | DC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA D 307 |
| Chain | Residue |
| B | PRO32 |
| B | VAL33 |
| D | ASP70 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00388 |
| Chain | Residue | Details |
| A | HIS264 | |
| B | HIS264 | |
| C | HIS264 | |
| D | HIS264 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00388 |
| Chain | Residue | Details |
| A | HIS78 | |
| D | HIS78 | |
| D | HIS237 | |
| D | ASP241 | |
| A | HIS237 | |
| A | ASP241 | |
| B | HIS78 | |
| B | HIS237 | |
| B | ASP241 | |
| C | HIS78 | |
| C | HIS237 | |
| C | ASP241 |
