3EWD
Crystal structure of adenosine deaminase mutant (delta Asp172) from Plasmodium vivax in complex with MT-coformycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004000 | molecular_function | adenosine deaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006154 | biological_process | adenosine catabolic process |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
| A | 0009897 | cellular_component | external side of plasma membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019239 | molecular_function | deaminase activity |
| A | 0043103 | biological_process | hypoxanthine salvage |
| A | 0046103 | biological_process | inosine biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0060169 | biological_process | negative regulation of adenosine receptor signaling pathway |
| A | 0090614 | molecular_function | 5'-methylthioadenosine deaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 371 |
| Chain | Residue |
| A | HIS42 |
| A | HIS44 |
| A | HIS225 |
| A | ASP309 |
| A | MCF372 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MCF A 372 |
| Chain | Residue |
| A | PHE88 |
| A | PHE132 |
| A | GLY200 |
| A | HIS225 |
| A | GLU228 |
| A | HIS252 |
| A | ASP309 |
| A | ASP310 |
| A | ZN371 |
| A | HOH443 |
| A | HIS44 |
| A | ASP46 |
| A | LEU47 |
| A | LEU85 |
Functional Information from PROSITE/UniProt
| site_id | PS00485 |
| Number of Residues | 7 |
| Details | A_DEAMINASE Adenosine and AMP deaminase signature. SVNSDDP |
| Chain | Residue | Details |
| A | SER305-PRO311 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18602399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19728741","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EWC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EWD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18602399","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QVN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18602399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19728741","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EWD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18602399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19728741","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PGR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EWC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EWD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
