4YML
Crystal structure of Escherichia coli 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with (3S,4R)-methylthio-DADMe-Immucillin-A
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue 4F0 A 301 |
| Chain | Residue |
| A | GLU12 |
| A | MET173 |
| A | GLU174 |
| A | SER196 |
| A | ASP197 |
| A | ILE50 |
| A | SER76 |
| A | ALA77 |
| A | GLY78 |
| A | ALA150 |
| A | PHE151 |
| A | ILE152 |
| A | GLU172 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 302 |
| Chain | Residue |
| A | MET1 |
| A | GLY154 |
| A | SER155 |
| A | LEU158 |
| A | ASP200 |
| A | GLN201 |
| A | HOH410 |
| A | HOH416 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 | 1 |
| 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 | 2 |
| 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 | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
