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 | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019239 | molecular_function | deaminase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046936 | molecular_function | 2'-deoxyadenosine deaminase activity |
| 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: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:3EWC, ECO:0007744|PDB:3EWD |
| Chain | Residue | Details |
| A | HIS42 | |
| A | HIS44 | |
| A | ALA226 | |
| A | GLY253 | |
| A | ASP310 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWC |
| Chain | Residue | Details |
| A | THR172 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWD |
| Chain | Residue | Details |
| A | HIS201 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWC, ECO:0007744|PDB:3EWD |
| Chain | Residue | Details |
| A | ASP229 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Important for substrate specificity for S-methyl-5'-thioadenosine => ECO:0000269|PubMed:19728741 |
| Chain | Residue | Details |
| A | THR172 |
