4X24
Crystal structure of Vibrio cholerae 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with methylthio-DADMe-Immucillin-A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005829 | cellular_component | cytosol |
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 | 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 | 14 |
Details | binding site for residue TDI A 301 |
Chain | Residue |
A | ILE50 |
A | GLU175 |
A | SER197 |
A | ASP198 |
A | PHE208 |
A | HOH453 |
A | SER76 |
A | ALA77 |
A | GLY78 |
A | ALA151 |
A | PHE152 |
A | ILE153 |
A | GLU173 |
A | MET174 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue PGE A 302 |
Chain | Residue |
A | GLN131 |
A | GLN135 |
A | HOH418 |
A | HOH419 |
A | HOH428 |
B | PRO167 |
B | SER168 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue TDI B 301 |
Chain | Residue |
B | ILE50 |
B | SER76 |
B | ALA77 |
B | GLY78 |
B | ALA151 |
B | PHE152 |
B | ILE153 |
B | GLU173 |
B | MET174 |
B | GLU175 |
B | SER197 |
B | ASP198 |
B | PHE208 |
B | HOH475 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684 |
Chain | Residue | Details |
A | GLU12 | |
B | GLU12 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01684 |
Chain | Residue | Details |
A | ASP198 | |
B | ASP198 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684 |
Chain | Residue | Details |
A | GLY78 | |
A | ILE153 | |
A | MET174 | |
B | GLY78 | |
B | ILE153 | |
B | MET174 |