5UE1
Crystal structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase in complex with adenine from Vibrio fischeri ES114
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 | 0016787 | molecular_function | hydrolase activity |
| A | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| 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 | 0016787 | molecular_function | hydrolase activity |
| B | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue 9DA A 301 |
| Chain | Residue |
| A | ALA77 |
| A | TRS302 |
| A | GLY78 |
| A | VAL151 |
| A | PHE152 |
| A | VAL153 |
| A | GLU173 |
| A | SER197 |
| A | ASP198 |
| A | ALA200 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue TRS A 302 |
| Chain | Residue |
| A | MET9 |
| A | GLU12 |
| A | SER76 |
| A | PHE152 |
| A | GLU173 |
| A | MET174 |
| A | GLU175 |
| A | ARG194 |
| A | PHE208 |
| A | 9DA301 |
| A | HOH516 |
| B | EDO306 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CA A 303 |
| Chain | Residue |
| A | ASN-1 |
| A | HOH597 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 304 |
| Chain | Residue |
| A | ASP18 |
| A | HOH559 |
| A | HOH647 |
| B | ASP18 |
| B | HOH549 |
| B | HOH609 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 305 |
| Chain | Residue |
| A | MET206 |
| A | ASP209 |
| A | GLU210 |
| A | HOH598 |
| A | HOH609 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | MET9 |
| A | GLU10 |
| A | GLN11 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 307 |
| Chain | Residue |
| A | VAL142 |
| A | ARG143 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue 9DA B 301 |
| Chain | Residue |
| B | ALA77 |
| B | GLY78 |
| B | VAL151 |
| B | PHE152 |
| B | VAL153 |
| B | GLU173 |
| B | SER197 |
| B | ASP198 |
| B | ALA200 |
| B | TRS302 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue TRS B 302 |
| Chain | Residue |
| B | ALA8 |
| B | MET9 |
| B | GLU12 |
| B | SER76 |
| B | PHE152 |
| B | GLU173 |
| B | MET174 |
| B | GLU175 |
| B | ARG194 |
| B | PHE208 |
| B | 9DA301 |
| B | HOH486 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 303 |
| Chain | Residue |
| A | MET112 |
| A | GLN181 |
| B | ILE50 |
| B | GLY51 |
| B | VAL53 |
| B | ALA54 |
| B | HOH463 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 304 |
| Chain | Residue |
| B | GLU10 |
| B | GLN11 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 305 |
| Chain | Residue |
| B | VAL142 |
| B | ARG143 |
| B | HOH464 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| A | TRS302 |
| B | PHE105 |
| B | HOH451 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
