4YO8
Crystal structure of Helicobacter pylori 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with (((4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)(hexyl)amino)methanol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
| 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 | 0005829 | cellular_component | cytosol |
| 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 | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
| 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 | 13 |
| Details | binding site for residue 4EZ A 301 |
| Chain | Residue |
| A | VAL79 |
| A | SER198 |
| A | ASP199 |
| A | HOH410 |
| B | PHE108 |
| A | ALA80 |
| A | GLY81 |
| A | PHE154 |
| A | VAL155 |
| A | VAL173 |
| A | GLU174 |
| A | MET175 |
| A | GLU176 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | GLU211 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue 4EZ B 301 |
| Chain | Residue |
| A | PHE108 |
| B | VAL79 |
| B | ALA80 |
| B | GLY81 |
| B | PHE154 |
| B | VAL155 |
| B | GLU174 |
| B | MET175 |
| B | GLU176 |
| B | SER198 |
| B | ASP199 |
| B | PHE209 |
| B | HOH416 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20954236 |
| Chain | Residue | Details |
| A | GLU14 | |
| B | GLU14 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:20954236 |
| Chain | Residue | Details |
| A | ASP199 | |
| B | ASP199 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY81 | |
| B | GLY81 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | VAL155 | |
| A | MET175 | |
| B | VAL155 | |
| B | MET175 |
