4IMD
Crystal Structure of Pasteurella multocida N-Acetyl-D-Neuraminic acid lyase trapped with pyruvate covalently bound through a Schiff base to Lys164
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 PO4 A 301 |
| Chain | Residue |
| A | ALA179 |
| A | TYR180 |
| A | PRO181 |
| A | ASN182 |
| A | HIS183 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | ASN182 |
| A | HOH577 |
| A | HOH579 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | GLU191 |
| A | HOH580 |
| A | HOH593 |
| A | ASP190 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | GLY226 |
| A | LEU228 |
| A | LYS229 |
| A | HOH581 |
| B | GLN224 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 305 |
| Chain | Residue |
| A | LYS2 |
| A | TYR132 |
| A | HOH522 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 301 |
| Chain | Residue |
| B | ALA179 |
| B | TYR180 |
| B | PRO181 |
| B | ASN182 |
| B | HIS183 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| Chain | Residue |
| B | ASP190 |
| B | GLU191 |
| B | HOH568 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| B | LEU161 |
| B | ASN182 |
| B | HOH524 |
| B | HOH600 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 C 301 |
| Chain | Residue |
| C | TYR180 |
| C | PRO181 |
| C | ASN182 |
| C | HIS183 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 302 |
| Chain | Residue |
| C | THR107 |
| C | SER137 |
| C | ILE138 |
| C | PRO139 |
| C | THR142 |
| C | VAL144 |
| C | ILE146 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 303 |
| Chain | Residue |
| C | PHE189 |
| C | ASP190 |
| C | GLU191 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 D 301 |
| Chain | Residue |
| D | TYR180 |
| D | PRO181 |
| D | ASN182 |
| D | HIS183 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 302 |
| Chain | Residue |
| D | THR107 |
| D | TYR136 |
| D | SER137 |
| D | ILE138 |
| D | PRO139 |
| D | THR142 |
| D | VAL144 |
| D | ILE146 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 303 |
| Chain | Residue |
| D | ASP190 |
| D | GLU191 |
| D | HOH565 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D 304 |
| Chain | Residue |
| D | LEU161 |
| D | ASN182 |
Functional Information from PROSITE/UniProt
| site_id | PS00217 |
| Number of Residues | 26 |
| Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. VdGLYvGGstgenfmLstEekkeifR |
| Chain | Residue | Details |
| A | VAL39-ARG64 |
| site_id | PS00665 |
| Number of Residues | 18 |
| Details | DHDPS_1 Dihydrodipicolinate synthase signature 1. GLYvgGSTGENfmlsteE |
| Chain | Residue | Details |
| A | GLY41-GLU58 |
| site_id | PS00666 |
| Number of Residues | 31 |
| Details | DHDPS_2 Dihydrodipicolinate synthase signature 2. YSIPflTgvnIgveqfgelyknpk.VlGVKFT |
| Chain | Residue | Details |
| A | TYR136-THR166 |
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":"24152047","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24152047","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IMF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
