6DYY
Crystal structure of Helicobacter pylori 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with (3R,4S)-1-((4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)-4-(((3-(1-butyl-1H-1,2,3-triazol-4-yl)propyl)thio)methyl)pyrrolidin-3-ol
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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| 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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| C | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| C | 0009086 | biological_process | methionine biosynthetic process |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0009164 | biological_process | nucleoside catabolic process |
| C | 0009234 | biological_process | menaquinone biosynthetic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
| C | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| C | 0102246 | molecular_function | 6-amino-6-deoxyfutalosine hydrolase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| D | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| D | 0009086 | biological_process | methionine biosynthetic process |
| D | 0009116 | biological_process | nucleoside metabolic process |
| D | 0009164 | biological_process | nucleoside catabolic process |
| D | 0009234 | biological_process | menaquinone biosynthetic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
| D | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| D | 0102246 | molecular_function | 6-amino-6-deoxyfutalosine hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | THR123 |
| A | GLY125 |
| A | SER126 |
| A | HOH464 |
| C | ASP209 |
| D | PHE107 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | HOH418 |
| A | HOH428 |
| A | HOH579 |
| A | HOH591 |
| A | GLU229 |
| A | HOH401 |
| A | HOH403 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue OS6 A 303 |
| Chain | Residue |
| A | ILE52 |
| A | VAL78 |
| A | ALA79 |
| A | GLY80 |
| A | GLN152 |
| A | PHE153 |
| A | VAL154 |
| A | VAL172 |
| A | GLU173 |
| A | MET174 |
| A | GLU175 |
| A | SER197 |
| A | ASP198 |
| A | ALA200 |
| A | PHE208 |
| A | HOH416 |
| B | HIS109 |
| B | PRO115 |
| B | GLU116 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | THR123 |
| B | GLY125 |
| B | SER126 |
| B | HOH403 |
| B | HOH562 |
| C | PHE107 |
| D | ASP209 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| A | ALA106 |
| A | PHE107 |
| B | GLY205 |
| B | MET206 |
| B | ASP209 |
| B | HOH457 |
| B | HOH492 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | GLN138 |
| B | HIS139 |
| B | SER165 |
| B | GLU166 |
| B | HOH536 |
| B | HOH546 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 304 |
| Chain | Residue |
| B | LYS133 |
| B | HOH401 |
| B | HOH411 |
| B | HOH424 |
| B | HOH453 |
| B | HOH585 |
| B | HOH601 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | binding site for residue OS6 B 305 |
| Chain | Residue |
| A | LEU104 |
| A | HIS109 |
| A | PRO115 |
| B | ALA9 |
| B | ILE52 |
| B | VAL78 |
| B | ALA79 |
| B | GLY80 |
| B | GLN152 |
| B | PHE153 |
| B | VAL154 |
| B | VAL172 |
| B | GLU173 |
| B | MET174 |
| B | GLU175 |
| B | SER197 |
| B | ASP198 |
| B | PHE208 |
| B | HOH423 |
| C | LYS132 |
| C | HOH483 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| C | GLY32 |
| C | ASN33 |
| C | VAL34 |
| C | TYR49 |
| C | HOH478 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| A | LYS157 |
| C | SER156 |
| C | LYS157 |
| C | ASP201 |
| C | GLU202 |
| C | HOH413 |
| site_id | AD2 |
| Number of Residues | 19 |
| Details | binding site for residue OS6 C 303 |
| Chain | Residue |
| C | VAL154 |
| C | VAL172 |
| C | GLU173 |
| C | MET174 |
| C | GLU175 |
| C | SER197 |
| C | ASP198 |
| C | PHE208 |
| C | HOH417 |
| D | PHE107 |
| D | HIS109 |
| A | GLU122 |
| C | ALA9 |
| C | ILE52 |
| C | VAL78 |
| C | ALA79 |
| C | GLY80 |
| C | GLN152 |
| C | PHE153 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 301 |
| Chain | Residue |
| D | GLY32 |
| D | ASN33 |
| D | VAL34 |
| D | TYR49 |
| D | HOH446 |
| site_id | AD4 |
| Number of Residues | 16 |
| Details | binding site for residue OS6 D 302 |
| Chain | Residue |
| C | HIS109 |
| D | ALA9 |
| D | ILE52 |
| D | VAL78 |
| D | ALA79 |
| D | GLY80 |
| D | PHE153 |
| D | VAL154 |
| D | VAL172 |
| D | GLU173 |
| D | MET174 |
| D | GLU175 |
| D | SER197 |
| D | ASP198 |
| D | PHE208 |
| D | HOH410 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 4 |
| 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 | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |






