2WO5
Structure of wild type E. coli N-acetylneuraminic acid lyase in space group P21 crystal form I
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 |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044010 | biological_process | single-species biofilm formation |
| 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 |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044010 | biological_process | single-species biofilm formation |
| 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 |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0044010 | biological_process | single-species biofilm formation |
| 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 |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0044010 | biological_process | single-species biofilm formation |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:24521460 |
| Chain | Residue | Details |
| A | TYR137 | |
| B | TYR137 | |
| C | TYR137 | |
| D | TYR137 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:12711733, ECO:0000269|PubMed:19923724, ECO:0000269|PubMed:24521460, ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:8081752 |
| Chain | Residue | Details |
| A | LYS165 | |
| B | LYS165 | |
| C | LYS165 | |
| D | LYS165 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9047371, ECO:0000305|PubMed:12711733, ECO:0007744|PDB:1FDY, ECO:0007744|PDB:1FDZ, ECO:0007744|PDB:1HL2 |
| Chain | Residue | Details |
| A | SER47 | |
| A | THR48 | |
| B | SER47 | |
| B | THR48 | |
| C | SER47 | |
| C | THR48 | |
| D | SER47 | |
| D | THR48 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24521460, ECO:0007744|PDB:4BWL |
| Chain | Residue | Details |
| A | THR167 | |
| B | SER208 | |
| C | THR167 | |
| C | GLY189 | |
| C | ASP191 | |
| C | GLU192 | |
| C | SER208 | |
| D | THR167 | |
| D | GLY189 | |
| D | ASP191 | |
| D | GLU192 | |
| A | GLY189 | |
| D | SER208 | |
| A | ASP191 | |
| A | GLU192 | |
| A | SER208 | |
| B | THR167 | |
| B | GLY189 | |
| B | ASP191 | |
| B | GLU192 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | SITE: Required to correctly position the proton donor => ECO:0000305|PubMed:24521460 |
| Chain | Residue | Details |
| A | SER47 | |
| A | TYR110 | |
| B | SER47 | |
| B | TYR110 | |
| C | SER47 | |
| C | TYR110 | |
| D | SER47 | |
| D | TYR110 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 553 |
| Chain | Residue | Details |
| A | TYR137 | proton acceptor, proton donor, proton relay |
| A | LYS165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 553 |
| Chain | Residue | Details |
| B | TYR137 | proton acceptor, proton donor, proton relay |
| B | LYS165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 553 |
| Chain | Residue | Details |
| C | TYR137 | proton acceptor, proton donor, proton relay |
| C | LYS165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 553 |
| Chain | Residue | Details |
| D | TYR137 | proton acceptor, proton donor, proton relay |
| D | LYS165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |
