3BSF
Crystal Structure of the MTA/SAH nucleosidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0009507 | cellular_component | chloroplast |
| A | 0010087 | biological_process | phloem or xylem histogenesis |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0009507 | cellular_component | chloroplast |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE ADE A 701 |
| Chain | Residue |
| A | MET168 |
| A | LYS186 |
| A | THR211 |
| A | ASP212 |
| A | HOH704 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADE B 702 |
| Chain | Residue |
| B | ASP187 |
| B | THR211 |
| B | ASP212 |
| B | VAL214 |
| B | PHE224 |
| B | HOH707 |
| B | ALA104 |
| B | GLY105 |
| B | MET168 |
| B | LYS186 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9T0I8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q9T0I8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9T0I8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19249293","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
