5DRO
Structure of the Aquifex aeolicus LpxC/LPC-011 Complex
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 | 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 | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006629 | biological_process | lipid 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | HIS74 |
| A | HIS226 |
| A | ASP230 |
| A | ZH2402 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue ZH2 A 402 |
| Chain | Residue |
| A | ALA181 |
| A | GLY198 |
| A | SER199 |
| A | HIS226 |
| A | LYS227 |
| A | ASP230 |
| A | HIS253 |
| A | ZN401 |
| A | HOH504 |
| A | HIS58 |
| A | GLU73 |
| A | HIS74 |
| A | THR179 |
| A | PHE180 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue DMS A 403 |
| Chain | Residue |
| B | HIS29 |
| B | GLU90 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | HIS74 |
| B | HIS226 |
| B | ASP230 |
| B | ZH2402 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue ZH2 B 402 |
| Chain | Residue |
| B | HIS19 |
| B | HIS58 |
| B | GLU73 |
| B | HIS74 |
| B | THR179 |
| B | ILE189 |
| B | GLY198 |
| B | SER199 |
| B | THR203 |
| B | HIS226 |
| B | LYS227 |
| B | ASP230 |
| B | HIS253 |
| B | ZN401 |
| B | DMS404 |
| B | HOH520 |
| B | HOH645 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 403 |
| Chain | Residue |
| B | LYS140 |
| B | GLU142 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue DMS B 404 |
| Chain | Residue |
| B | THR56 |
| B | HIS58 |
| B | LYS227 |
| B | GLY252 |
| B | HIS253 |
| B | ZH2402 |
| B | HOH582 |
| B | HOH596 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15705580","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00388","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12819349","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15705580","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P42","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YH8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YHC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
