5ZJM
Crystal structure of N-acetylneuraminate lyase from Fusobacterium nucleatum
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 EDO A 301 |
Chain | Residue |
A | ASN13 |
A | ILE18 |
A | ASN19 |
A | GLU20 |
A | LYS21 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO B 301 |
Chain | Residue |
B | LYS21 |
B | ASN13 |
B | ILE18 |
B | ASN19 |
B | GLU20 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO C 301 |
Chain | Residue |
C | ASN13 |
C | ILE18 |
C | ASN19 |
C | GLU20 |
C | LYS21 |
Functional Information from PROSITE/UniProt
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 | TYR133 | |
B | TYR133 | |
C | TYR133 | |
D | TYR133 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_01237, ECO:0000305|PubMed:30387778 |
Chain | Residue | Details |
A | LYS161 | |
B | LYS161 | |
C | LYS161 | |
D | LYS161 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01237 |
Chain | Residue | Details |
A | SER44 | |
B | THR163 | |
B | GLY185 | |
B | ASP187 | |
B | GLU188 | |
B | SER204 | |
C | SER44 | |
C | THR45 | |
C | THR163 | |
C | GLY185 | |
C | ASP187 | |
A | THR45 | |
C | GLU188 | |
C | SER204 | |
D | SER44 | |
D | THR45 | |
D | THR163 | |
D | GLY185 | |
D | ASP187 | |
D | GLU188 | |
D | SER204 | |
A | THR163 | |
A | GLY185 | |
A | ASP187 | |
A | GLU188 | |
A | SER204 | |
B | SER44 | |
B | THR45 |