6PO4
2.1 Angstrom Resolution Crystal Structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (mtnN) from Haemophilus influenzae PittII.
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 | 0009116 | biological_process | nucleoside metabolic process |
| A | 0009164 | biological_process | nucleoside catabolic process |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| B | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0009164 | biological_process | nucleoside catabolic process |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| C | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0009164 | biological_process | nucleoside catabolic process |
| C | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| D | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| D | 0009116 | biological_process | nucleoside metabolic process |
| D | 0009164 | biological_process | nucleoside catabolic process |
| D | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| E | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| E | 0009116 | biological_process | nucleoside metabolic process |
| E | 0009164 | biological_process | nucleoside catabolic process |
| E | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
| F | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| F | 0009116 | biological_process | nucleoside metabolic process |
| F | 0009164 | biological_process | nucleoside catabolic process |
| F | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue HCS A 301 |
| Chain | Residue |
| A | PHE105 |
| C | ASN39 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue ADE A 302 |
| Chain | Residue |
| A | MET173 |
| A | SER196 |
| A | ASP197 |
| A | GLY199 |
| A | BO3303 |
| A | SER76 |
| A | ALA77 |
| A | GLY78 |
| A | SER150 |
| A | PHE151 |
| A | ILE152 |
| A | GLU172 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue BO3 A 303 |
| Chain | Residue |
| A | ALA8 |
| A | GLU12 |
| A | SER76 |
| A | GLU172 |
| A | MET173 |
| A | GLU174 |
| A | ARG193 |
| A | ADE302 |
| A | HOH413 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue ADE B 301 |
| Chain | Residue |
| B | ALA77 |
| B | GLY78 |
| B | SER150 |
| B | PHE151 |
| B | ILE152 |
| B | GLU172 |
| B | SER196 |
| B | ASP197 |
| B | GLY199 |
| B | BO3303 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue HCS B 302 |
| Chain | Residue |
| B | PHE105 |
| B | TYR107 |
| E | GLU208 |
| F | HCS302 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue BO3 B 303 |
| Chain | Residue |
| B | GLU12 |
| B | SER76 |
| B | GLU172 |
| B | MET173 |
| B | GLU174 |
| B | ARG193 |
| B | ADE301 |
| B | HOH407 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue ADE C 301 |
| Chain | Residue |
| C | ALA77 |
| C | GLY78 |
| C | SER150 |
| C | PHE151 |
| C | ILE152 |
| C | GLU172 |
| C | MET173 |
| C | SER196 |
| C | ASP197 |
| C | GLY199 |
| C | BO3304 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue HCS C 302 |
| Chain | Residue |
| C | PHE105 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue HCS C 303 |
| Chain | Residue |
| C | ILE50 |
| D | TYR107 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue BO3 C 304 |
| Chain | Residue |
| C | GLU12 |
| C | SER76 |
| C | GLU172 |
| C | MET173 |
| C | GLU174 |
| C | ARG193 |
| C | ADE301 |
| C | HOH411 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue ADE D 301 |
| Chain | Residue |
| D | ALA77 |
| D | GLY78 |
| D | SER150 |
| D | PHE151 |
| D | ILE152 |
| D | GLU172 |
| D | SER196 |
| D | ASP197 |
| D | GLY199 |
| D | BO3302 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue BO3 D 302 |
| Chain | Residue |
| D | GLU12 |
| D | SER76 |
| D | GLU172 |
| D | MET173 |
| D | GLU174 |
| D | ARG193 |
| D | ADE301 |
| D | HOH411 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue ADE E 301 |
| Chain | Residue |
| E | ALA77 |
| E | GLY78 |
| E | SER150 |
| E | PHE151 |
| E | ILE152 |
| E | GLU172 |
| E | MET173 |
| E | SER196 |
| E | ASP197 |
| E | GLY199 |
| E | BO3303 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue HCS E 302 |
| Chain | Residue |
| A | ASN39 |
| E | PHE105 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue BO3 E 303 |
| Chain | Residue |
| E | SER76 |
| E | GLU172 |
| E | MET173 |
| E | GLU174 |
| E | ARG193 |
| E | ADE301 |
| E | HOH409 |
| E | GLU12 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue ADE F 301 |
| Chain | Residue |
| F | SER76 |
| F | ALA77 |
| F | GLY78 |
| F | SER150 |
| F | PHE151 |
| F | ILE152 |
| F | GLU172 |
| F | MET173 |
| F | SER196 |
| F | ASP197 |
| F | GLY199 |
| F | BO3303 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue HCS F 302 |
| Chain | Residue |
| A | GLU208 |
| B | HCS302 |
| E | ILE50 |
| F | TYR107 |
| F | HOH461 |
| site_id | AD9 |
| Number of Residues | 9 |
| Details | binding site for residue BO3 F 303 |
| Chain | Residue |
| F | ALA8 |
| F | GLU12 |
| F | SER76 |
| F | GLU172 |
| F | MET173 |
| F | GLU174 |
| F | ARG193 |
| F | ADE301 |
| F | HOH406 |
