3O4V
Crystal structure of E. coli MTA/SAH nucleosidase in complex with (4-Chlorophenyl)thio-DADMe-ImmA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046124 | biological_process | purine deoxyribonucleoside catabolic process |
| A | 0110052 | biological_process | toxic metabolite repair |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046124 | biological_process | purine deoxyribonucleoside catabolic process |
| B | 0110052 | biological_process | toxic metabolite repair |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 4CT A 233 |
| Chain | Residue |
| A | ILE50 |
| A | GLU174 |
| A | SER196 |
| A | ASP197 |
| A | PHE207 |
| A | HOH237 |
| B | TYR107 |
| A | SER76 |
| A | ALA77 |
| A | GLY78 |
| A | ALA150 |
| A | PHE151 |
| A | ILE152 |
| A | GLU172 |
| A | MET173 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 235 |
| Chain | Residue |
| A | PHE151 |
| A | ASN153 |
| A | GLY154 |
| A | SER155 |
| A | VAL156 |
| A | GLY157 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 236 |
| Chain | Residue |
| A | HIS180 |
| A | ASN184 |
| A | HOH300 |
| A | HOH370 |
| B | ALA54 |
| B | HOH331 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 4CT B 234 |
| Chain | Residue |
| A | PHE105 |
| A | TYR107 |
| B | ILE50 |
| B | SER76 |
| B | ALA77 |
| B | GLY78 |
| B | PHE105 |
| B | ALA150 |
| B | PHE151 |
| B | ILE152 |
| B | GLU172 |
| B | MET173 |
| B | GLU174 |
| B | SER196 |
| B | ASP197 |
| B | PHE207 |
| B | HOH246 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 237 |
| Chain | Residue |
| A | GLU94 |
| A | ARG96 |
| A | ALA117 |
| A | GLY118 |
| A | LYS120 |
| A | HOH364 |
| B | ARG96 |
| B | GLU108 |
| B | ALA117 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 238 |
| Chain | Residue |
| A | ASP208 |
| A | LEU211 |
| A | HOH238 |
| A | HOH305 |
| B | PHE207 |
| B | ASP208 |
| B | HOH289 |
| B | HOH327 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPA B 233 |
| Chain | Residue |
| A | HIS65 |
| A | HOH268 |
| A | HOH334 |
| A | HOH346 |
| B | ARG162 |
| B | HOH382 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16109423","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16109423","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11591349","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
