4G89
Crystal structure of k. pneumoniae mta/adohcy nucleosidase in complex with fragmented s-adenosyl-l-homocysteine
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 |
A | 0046124 | biological_process | purine deoxyribonucleoside catabolic process |
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 |
B | 0046124 | biological_process | purine deoxyribonucleoside catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ADE A 301 |
Chain | Residue |
A | ALA77 |
A | SAH302 |
A | GLY78 |
A | ALA150 |
A | PHE151 |
A | ILE152 |
A | GLU172 |
A | SER196 |
A | ASP197 |
A | ALA199 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH A 302 |
Chain | Residue |
A | ALA8 |
A | MET9 |
A | ILE50 |
A | SER76 |
A | ALA135 |
A | LEU136 |
A | PHE151 |
A | GLU172 |
A | MET173 |
A | GLU174 |
A | ARG193 |
A | PHE207 |
A | ADE301 |
A | HOH460 |
B | PHE105 |
B | TYR107 |
B | PRO113 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | GLY154 |
A | SER155 |
A | LEU158 |
A | ASP200 |
A | GLN201 |
A | HOH535 |
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 | ASP197 | |
B | ASP197 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684 |
Chain | Residue | Details |
A | MET173 | |
B | GLY78 | |
B | ILE152 | |
B | MET173 | |
A | GLY78 | |
A | ILE152 |