6AYQ
Crystal structure of Campylobacter jejuni 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with methylthio-DADMe-Immucillin-A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| A | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0009164 | biological_process | nucleoside catabolic process |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| A | 0102246 | molecular_function | 6-amino-6-deoxyfutalosine hydrolase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| B | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0009164 | biological_process | nucleoside catabolic process |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0102246 | molecular_function | 6-amino-6-deoxyfutalosine hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue TDI A 301 |
| Chain | Residue |
| A | ALA8 |
| A | GLU171 |
| A | MET172 |
| A | GLU173 |
| A | SER195 |
| A | ASP196 |
| A | PHE206 |
| A | HOH420 |
| B | ILE102 |
| B | PHE105 |
| A | ILE50 |
| A | VAL76 |
| A | ALA77 |
| A | GLY78 |
| A | GLU150 |
| A | PHE151 |
| A | ILE152 |
| A | CYS170 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue TDI B 301 |
| Chain | Residue |
| A | ILE102 |
| A | PHE105 |
| B | ALA8 |
| B | ILE50 |
| B | VAL76 |
| B | ALA77 |
| B | GLY78 |
| B | GLU150 |
| B | PHE151 |
| B | ILE152 |
| B | CYS170 |
| B | GLU171 |
| B | MET172 |
| B | GLU173 |
| B | SER195 |
| B | ASP196 |
| B | PHE206 |
| B | HOH417 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| A | GLU116 |
| A | ASP207 |
| B | PHE105 |
| B | HIS107 |
| B | PRO113 |
| B | HOH410 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU12 | |
| B | GLU12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP196 | |
| B | ASP196 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY78 | |
| A | ILE152 | |
| A | MET172 | |
| B | GLY78 | |
| B | ILE152 | |
| B | MET172 |
