6DYV
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-((pent-4-yn-1-ylthio)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 | 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 | 8 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | SER124 |
| A | GLY125 |
| A | SER126 |
| A | HOH406 |
| A | HOH560 |
| B | PHE107 |
| B | ASP209 |
| B | OS3305 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | ASN33 |
| A | VAL34 |
| A | TYR49 |
| A | HOH438 |
| A | GLY32 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | GLN138 |
| A | HIS139 |
| A | SER165 |
| A | GLU166 |
| A | HOH541 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ARG159 |
| A | HOH463 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | LYS157 |
| A | GLU158 |
| A | GLU161 |
| A | HOH439 |
| B | GLU202 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue OS3 A 306 |
| Chain | Residue |
| A | ALA9 |
| A | MET10 |
| A | ILE52 |
| A | VAL78 |
| A | ALA79 |
| A | GLY80 |
| A | LEU104 |
| A | PHE107 |
| A | GLN152 |
| A | PHE153 |
| A | VAL154 |
| A | GLU173 |
| A | MET174 |
| A | GLU175 |
| A | SER197 |
| A | ASP198 |
| A | ALA200 |
| A | PHE208 |
| A | HOH420 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | GLY32 |
| B | ASN33 |
| B | VAL34 |
| B | TYR49 |
| B | HOH462 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | GLN152 |
| B | ARG159 |
| B | HOH515 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| A | SER126 |
| B | ALA106 |
| B | MET206 |
| B | HOH413 |
| B | HOH435 |
| B | HOH457 |
| B | HOH591 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| A | GLN71 |
| A | LYS72 |
| A | PRO189 |
| A | HOH403 |
| B | GLU210 |
| B | HOH401 |
| B | HOH466 |
| site_id | AD2 |
| Number of Residues | 19 |
| Details | binding site for residue OS3 B 305 |
| Chain | Residue |
| A | EDO301 |
| B | ALA9 |
| B | ILE52 |
| B | VAL78 |
| B | ALA79 |
| B | GLY80 |
| B | LEU104 |
| B | PHE153 |
| B | VAL154 |
| B | VAL172 |
| B | GLU173 |
| B | MET174 |
| B | GLU175 |
| B | SER197 |
| B | ASP198 |
| B | ALA200 |
| B | PHE208 |
| B | ASP209 |
| B | HOH426 |
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 | GLU13 | |
| B | GLU13 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:20954236 |
| Chain | Residue | Details |
| A | ASP198 | |
| B | ASP198 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY80 | |
| B | GLY80 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | VAL154 | |
| B | MET174 | |
| A | VAL154 | |
| A | MET174 |
