4AHO
Crystal Structure of N-acetylneuraminic acid lyase from Staphylococcus aureus with the chemical modification thia-lysine at position 165
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 | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1294 |
| Chain | Residue |
| A | ALA11 |
| A | SER48 |
| A | SER49 |
| A | SLZ165 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1294 |
| Chain | Residue |
| B | ALA11 |
| B | SER48 |
| B | SER49 |
| B | SLZ165 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 1294 |
| Chain | Residue |
| C | SER48 |
| C | SER49 |
| C | SLZ165 |
| C | ALA11 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 1294 |
| Chain | Residue |
| D | ALA11 |
| D | SER48 |
| D | SER49 |
| D | SLZ165 |
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 |
