3BSF
Crystal Structure of the MTA/SAH nucleosidase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000003 | biological_process | obsolete reproduction |
A | 0003824 | molecular_function | catalytic activity |
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 | 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 | 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 | 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 | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9T0I8 |
Chain | Residue | Details |
A | GLU25 | |
B | GLU25 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9T0I8 |
Chain | Residue | Details |
A | ASP212 | |
B | ASP212 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9T0I8 |
Chain | Residue | Details |
A | THR103 | |
B | THR103 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19249293 |
Chain | Residue | Details |
A | LYS186 | |
A | ASP212 | |
B | LYS186 | |
B | ASP212 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |