5KZE
N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus
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 |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0005975 | biological_process | carbohydrate metabolic process |
E | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
E | 0016829 | molecular_function | lyase activity |
E | 0019262 | biological_process | N-acetylneuraminate catabolic process |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0005975 | biological_process | carbohydrate metabolic process |
F | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
F | 0016829 | molecular_function | lyase activity |
F | 0019262 | biological_process | N-acetylneuraminate catabolic process |
G | 0005737 | cellular_component | cytoplasm |
G | 0005829 | cellular_component | cytosol |
G | 0005975 | biological_process | carbohydrate metabolic process |
G | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
G | 0016829 | molecular_function | lyase activity |
G | 0019262 | biological_process | N-acetylneuraminate catabolic process |
H | 0005737 | cellular_component | cytoplasm |
H | 0005829 | cellular_component | cytosol |
H | 0005975 | biological_process | carbohydrate metabolic process |
H | 0008747 | molecular_function | N-acetylneuraminate lyase activity |
H | 0016829 | molecular_function | lyase activity |
H | 0019262 | biological_process | N-acetylneuraminate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 301 |
Chain | Residue |
A | ALA11 |
A | GLY47 |
A | SER48 |
A | SER49 |
A | TYR137 |
A | LYS165 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | HOH411 |
A | HOH427 |
A | ASP191 |
A | GLU192 |
A | SER208 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
B | ALA11 |
B | GLY47 |
B | SER48 |
B | SER49 |
B | TYR137 |
B | LYS165 |
B | HOH402 |
B | HOH417 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 302 |
Chain | Residue |
B | GLY189 |
B | PHE190 |
B | ASP191 |
B | GLU192 |
B | HOH401 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue SO4 C 301 |
Chain | Residue |
C | ALA11 |
C | TYR44 |
C | GLY47 |
C | SER48 |
C | SER49 |
C | TYR137 |
C | LYS165 |
C | HOH496 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL C 302 |
Chain | Residue |
C | SER49 |
C | GLU192 |
C | SER208 |
C | ILE251 |
C | TYR252 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue SO4 D 301 |
Chain | Residue |
D | ALA11 |
D | GLY47 |
D | SER48 |
D | SER49 |
D | TYR137 |
D | LYS165 |
D | HOH421 |
D | HOH437 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue GOL D 302 |
Chain | Residue |
D | PHE190 |
D | ASP191 |
D | GLU192 |
D | LEU247 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue SO4 E 301 |
Chain | Residue |
E | ALA11 |
E | GLY47 |
E | SER48 |
E | SER49 |
E | TYR137 |
E | LYS165 |
E | HOH417 |
E | HOH505 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue GOL E 302 |
Chain | Residue |
E | GLY189 |
E | LEU247 |
E | ILE251 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue SO4 F 301 |
Chain | Residue |
F | ALA11 |
F | TYR44 |
F | GLY47 |
F | SER48 |
F | SER49 |
F | TYR137 |
F | LYS165 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue GOL F 302 |
Chain | Residue |
F | PHE190 |
F | SER208 |
F | HOH401 |
F | HOH409 |
F | HOH463 |
F | HOH507 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue SO4 G 301 |
Chain | Residue |
G | ALA11 |
G | TYR44 |
G | GLY47 |
G | SER48 |
G | SER49 |
G | TYR137 |
G | LYS165 |
G | HOH413 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue GOL G 302 |
Chain | Residue |
G | GLU192 |
G | SER208 |
G | HOH456 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue SO4 H 301 |
Chain | Residue |
H | ALA11 |
H | TYR44 |
H | GLY47 |
H | SER48 |
H | SER49 |
H | TYR137 |
H | LYS165 |
H | HOH415 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue GOL H 302 |
Chain | Residue |
H | THR167 |
H | GLY189 |
H | GLU192 |
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 | 8 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01237 |
Chain | Residue | Details |
A | TYR137 | |
B | TYR137 | |
C | TYR137 | |
D | TYR137 | |
E | TYR137 | |
F | TYR137 | |
G | TYR137 | |
H | TYR137 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000269|PubMed:23418011 |
Chain | Residue | Details |
A | LYS165 | |
B | LYS165 | |
C | LYS165 | |
D | LYS165 | |
E | LYS165 | |
F | LYS165 | |
G | LYS165 | |
H | LYS165 |
site_id | SWS_FT_FI3 |
Number of Residues | 56 |
Details | BINDING: BINDING => ECO:0000305|PubMed:27943302, ECO:0007744|PDB:5KZD |
Chain | Residue | Details |
A | SER48 | |
B | ASP191 | |
B | GLU192 | |
B | SER208 | |
C | SER48 | |
C | SER49 | |
C | GLY189 | |
C | ASP191 | |
C | GLU192 | |
C | SER208 | |
D | SER48 | |
A | SER49 | |
D | SER49 | |
D | GLY189 | |
D | ASP191 | |
D | GLU192 | |
D | SER208 | |
E | SER48 | |
E | SER49 | |
E | GLY189 | |
E | ASP191 | |
E | GLU192 | |
A | GLY189 | |
E | SER208 | |
F | SER48 | |
F | SER49 | |
F | GLY189 | |
F | ASP191 | |
F | GLU192 | |
F | SER208 | |
G | SER48 | |
G | SER49 | |
G | GLY189 | |
A | ASP191 | |
G | ASP191 | |
G | GLU192 | |
G | SER208 | |
H | SER48 | |
H | SER49 | |
H | GLY189 | |
H | ASP191 | |
H | GLU192 | |
H | SER208 | |
A | TYR252 | |
A | GLU192 | |
B | TYR252 | |
C | TYR252 | |
D | TYR252 | |
E | TYR252 | |
F | TYR252 | |
G | TYR252 | |
H | TYR252 | |
A | SER208 | |
B | SER48 | |
B | SER49 | |
B | GLY189 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01237 |
Chain | Residue | Details |
A | THR167 | |
B | THR167 | |
C | THR167 | |
D | THR167 | |
E | THR167 | |
F | THR167 | |
G | THR167 | |
H | THR167 |