2WNN
Structure of wild type E. coli N-acetylneuraminic acid lyase in complex with pyruvate in space group P21
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 PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1PE B 1298 |
Chain | Residue |
B | PRO140 |
B | ALA141 |
B | GLY144 |
B | LYS146 |
B | HOH2109 |
C | ALA141 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1PE B 1299 |
Chain | Residue |
B | ASP170 |
B | GLN173 |
B | TYR190 |
B | GLU192 |
B | HOH2192 |
B | HOH2194 |
D | ASP170 |
B | PRO140 |
B | SER168 |
B | GLY169 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 1PE C 1297 |
Chain | Residue |
A | GLY169 |
A | GLU192 |
A | ILE193 |
C | GLY169 |
C | ASP170 |
C | LEU171 |
C | TYR172 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"24521460","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"12711733","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19923724","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24521460","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9047371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8081752","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"9047371","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12711733","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1FDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FDZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HL2","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"24521460","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BWL","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | Site: {"description":"Required to correctly position the proton donor","evidences":[{"source":"PubMed","id":"24521460","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
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 | KPI165 | 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 | KPI165 | 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 | KPI165 | 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 | KPI165 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor |