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 | 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 | SLZ165 | |
B | SLZ165 | |
C | SLZ165 | |
D | SLZ165 |
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 |