5LKY
X-ray crystal structure of N-acetylneuraminic acid lyase in complex with pyruvate, with the phenylalanine at position 190 replaced with the non-canonical amino acid dihydroxypropylcysteine.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019262 | biological_process | N-acetylneuraminate catabolic process |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019262 | biological_process | N-acetylneuraminate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 301 |
| Chain | Residue |
| A | ASP141 |
| A | GLY144 |
| D | ASP141 |
| D | LEU142 |
| D | GLY144 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue PEG B 301 |
| Chain | Residue |
| B | ASP141 |
| C | ASP141 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide GLY B 189 and P9S B 190 |
| Chain | Residue |
| B | THR167 |
| B | ALA168 |
| B | SER188 |
| B | ASP191 |
| B | GLU192 |
| B | MET193 |
| B | LEU194 |
| B | ILE206 |
| B | HOH401 |
| B | HOH402 |
| B | ASP141 |
| B | TYR166 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide P9S B 190 and ASP B 191 |
| Chain | Residue |
| B | ASP141 |
| B | THR167 |
| B | ALA168 |
| B | SER188 |
| B | GLY189 |
| B | GLU192 |
| B | MET193 |
| B | LEU194 |
| B | GLY207 |
| B | SER208 |
| B | THR209 |
| B | TYR210 |
| B | GLN236 |
| B | HOH401 |
| B | HOH402 |
| B | HOH440 |
| B | HOH457 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide GLY C 189 and P9S C 190 |
| Chain | Residue |
| C | ASP141 |
| C | TYR166 |
| C | THR167 |
| C | LEU187 |
| C | SER188 |
| C | ASP191 |
| C | GLU192 |
| C | MET193 |
| C | LEU194 |
| C | ILE206 |
| C | HOH303 |
| C | HOH324 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide P9S C 190 and ASP C 191 |
| Chain | Residue |
| C | ASP141 |
| C | SER188 |
| C | GLY189 |
| C | GLU192 |
| C | MET193 |
| C | LEU194 |
| C | GLY207 |
| C | SER208 |
| C | THR209 |
| C | TYR210 |
| C | GLN236 |
| C | HOH303 |
| C | HOH324 |
| C | HOH325 |
| C | HOH368 |
| C | HOH384 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide GLY D 189 and P9S D 190 |
| Chain | Residue |
| D | ASP141 |
| D | TYR166 |
| D | THR167 |
| D | ALA168 |
| D | SER188 |
| D | ASP191 |
| D | GLU192 |
| D | MET193 |
| D | LEU194 |
| D | ILE206 |
| D | HOH306 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide P9S D 190 and ASP D 191 |
| Chain | Residue |
| D | ASP141 |
| D | ALA168 |
| D | SER188 |
| D | GLY189 |
| D | GLU192 |
| D | MET193 |
| D | LEU194 |
| D | GLY207 |
| D | SER208 |
| D | THR209 |
| D | TYR210 |
| D | GLN236 |
| D | HOH306 |
| D | HOH343 |
| D | HOH372 |
Functional Information from PROSITE/UniProt
| site_id | PS00666 |
| Number of Residues | 31 |
| Details | DHDPS_2 Dihydrodipicolinate synthase signature 2. YAIPdlTgvnIsieqfselfnhek.IvGVKYT |
| Chain | Residue | Details |
| A | TYR137-THR167 |
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_01237","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"HAMAP-Rule","id":"MF_01237","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23418011","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27943302","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5KZD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
