2QTT
Crystal Structure of Arabidopsis thaliana 5'-Methylthioadenosine nucleosidase in complex with Formycin A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000003 | biological_process | obsolete reproduction |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0010087 | biological_process | phloem or xylem histogenesis |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0000003 | biological_process | obsolete reproduction |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0010087 | biological_process | phloem or xylem histogenesis |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ADE A 268 |
| Chain | Residue |
| A | CYS117 |
| A | GLY118 |
| A | LYS199 |
| A | ASP200 |
| A | MET201 |
| A | ASP225 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 270 |
| Chain | Residue |
| B | GLU188 |
| B | ASP228 |
| B | HOH458 |
| B | HIS66 |
| B | PHE120 |
| B | MET183 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FMC B 269 |
| Chain | Residue |
| B | THR116 |
| B | CYS117 |
| B | GLY118 |
| B | LEU181 |
| B | LYS199 |
| B | ASP200 |
| B | MET201 |
| B | GLU202 |
| B | THR224 |
| B | ASP225 |
| B | THR233 |
| B | PHE237 |
| B | HOH275 |
| B | HOH301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:20554051 |
| Chain | Residue | Details |
| A | GLU38 | |
| B | GLU38 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:20554051 |
| Chain | Residue | Details |
| A | ASP225 | |
| B | ASP225 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18342331, ECO:0000305|PubMed:20554051, ECO:0007744|PDB:2QTT, ECO:0007744|PDB:3LGS |
| Chain | Residue | Details |
| A | THR116 | |
| A | ASP225 | |
| B | THR116 | |
| B | ASP225 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16909418, ECO:0000269|PubMed:20554051, ECO:0007744|PDB:2H8G, ECO:0007744|PDB:3LGS |
| Chain | Residue | Details |
| A | LYS199 | |
| B | LYS199 |
