5N8C
Crystal structure of Pseudomonas aeruginosa LpxC complexed with inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0008759 | molecular_function | obsolete UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity |
| A | 0009245 | biological_process | lipid A biosynthetic process |
| 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 | 0008759 | molecular_function | obsolete UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | HIS78 |
| A | HIS237 |
| A | ASP241 |
| A | 8Q8403 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | GLU198 |
| A | 8Q8403 |
| B | GLU198 |
| B | ZN402 |
| B | 8Q8403 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue 8Q8 A 403 |
| Chain | Residue |
| A | LEU18 |
| A | HIS19 |
| A | MET62 |
| A | GLU77 |
| A | HIS78 |
| A | THR190 |
| A | PHE191 |
| A | MET194 |
| A | ILE197 |
| A | GLU198 |
| A | ARG201 |
| A | ALA206 |
| A | GLY209 |
| A | SER210 |
| A | HIS237 |
| A | ASP241 |
| A | HIS264 |
| A | ZN401 |
| A | ZN402 |
| A | HOH592 |
| A | HOH596 |
| B | GLU198 |
| B | ZN402 |
| B | 8Q8403 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | GLY263 |
| A | LEU266 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | HIS78 |
| B | HIS237 |
| B | ASP241 |
| B | 8Q8403 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 402 |
| Chain | Residue |
| A | GLU198 |
| A | ZN402 |
| A | 8Q8403 |
| B | GLU198 |
| B | 8Q8403 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue 8Q8 B 403 |
| Chain | Residue |
| A | GLU198 |
| A | ZN402 |
| A | 8Q8403 |
| B | HIS19 |
| B | MET62 |
| B | GLU77 |
| B | HIS78 |
| B | THR190 |
| B | PHE191 |
| B | MET194 |
| B | ILE197 |
| B | GLU198 |
| B | ARG201 |
| B | GLY209 |
| B | SER210 |
| B | HIS237 |
| B | ASP241 |
| B | HIS264 |
| B | ZN401 |
| B | ZN402 |
| B | HOH539 |
| B | HOH560 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 404 |
| Chain | Residue |
| B | GLY263 |
| B | LEU266 |
| B | HOH708 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00388 |
| Chain | Residue | Details |
| A | HIS264 | |
| B | HIS264 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00388 |
| Chain | Residue | Details |
| A | HIS78 | |
| A | HIS237 | |
| A | ASP241 | |
| B | HIS78 | |
| B | HIS237 | |
| B | ASP241 |
