4YNB
Crystal structure of Helicobacter pylori 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with pyrazinylthio-DADMe-Immucillin-A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue 4EH A 301 |
| Chain | Residue |
| A | ALA10 |
| A | VAL173 |
| A | GLU174 |
| A | MET175 |
| A | GLU176 |
| A | SER198 |
| A | ASP199 |
| A | ALA201 |
| A | PHE209 |
| A | HOH464 |
| A | HOH576 |
| A | ILE53 |
| A | VAL79 |
| A | ALA80 |
| A | GLY81 |
| A | LEU105 |
| A | HIS110 |
| A | PHE154 |
| A | VAL155 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | PHE114 |
| A | ALA119 |
| A | ILE120 |
| A | PHE121 |
| A | HOH549 |
| A | HOH558 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | HIS42 |
| A | ASN43 |
| A | LYS44 |
| A | LYS73 |
| A | HOH589 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 304 |
| Chain | Residue |
| A | GLN153 |
| A | GLN153 |
| A | HOH429 |
| A | HOH429 |
| A | HOH437 |
| A | HOH437 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"20954236","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20954236","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
