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 | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01237 |
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:0000255|HAMAP-Rule:MF_01237, ECO:0000269|PubMed:23418011 |
Chain | Residue | Details |
A | KPI165 | |
B | KPI165 | |
C | KPI165 | |
D | KPI165 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000305|PubMed:27943302, ECO:0007744|PDB:5KZD |
Chain | Residue | Details |
A | SER48 | |
B | GLY189 | |
B | ASP191 | |
B | GLU192 | |
B | SER208 | |
B | TYR252 | |
C | SER48 | |
C | SER49 | |
C | GLY189 | |
C | ASP191 | |
C | GLU192 | |
A | SER49 | |
C | SER208 | |
C | TYR252 | |
D | SER48 | |
D | SER49 | |
D | GLY189 | |
D | ASP191 | |
D | GLU192 | |
D | SER208 | |
D | TYR252 | |
A | GLY189 | |
A | ASP191 | |
A | GLU192 | |
A | SER208 | |
A | TYR252 | |
B | SER48 | |
B | SER49 |