2AMX
Crystal structure of Plasmodium Yoelii Adenosine deaminase (PY02076)
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 | 0019239 | molecular_function | deaminase activity |
A | 0043103 | biological_process | hypoxanthine salvage |
A | 0046103 | biological_process | inosine biosynthetic process |
A | 0060169 | biological_process | negative regulation of adenosine receptor signaling pathway |
B | 0004000 | molecular_function | adenosine deaminase activity |
B | 0005829 | cellular_component | cytosol |
B | 0006154 | biological_process | adenosine catabolic process |
B | 0006166 | biological_process | purine ribonucleoside salvage |
B | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
B | 0009897 | cellular_component | external side of plasma membrane |
B | 0019239 | molecular_function | deaminase activity |
B | 0043103 | biological_process | hypoxanthine salvage |
B | 0046103 | biological_process | inosine biosynthetic process |
B | 0060169 | biological_process | negative regulation of adenosine receptor signaling pathway |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CO A 1000 |
Chain | Residue |
A | HIS55 |
A | HIS57 |
A | HIS239 |
A | ASP323 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CO A 1002 |
Chain | Residue |
A | HIS177 |
A | GLU370 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CO B 1000 |
Chain | Residue |
B | ASP323 |
B | HIS55 |
B | HIS57 |
B | HIS239 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CO B 1001 |
Chain | Residue |
B | HIS212 |
B | LEU219 |
B | HIS222 |
B | HOH2177 |
B | HOH2205 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CO B 1002 |
Chain | Residue |
B | ASN174 |
B | HIS177 |
B | GLU370 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE UNX A 2000 |
Chain | Residue |
A | HIS212 |
A | ILE217 |
A | HIS222 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE UNX A 2001 |
Chain | Residue |
A | SER196 |
A | GLY197 |
A | PHE210 |
A | VAL225 |
A | HOH2109 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE UNX A 2003 |
Chain | Residue |
A | ASP185 |
A | GLY187 |
A | SER192 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE UNX A 2004 |
Chain | Residue |
A | HOH2047 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE UNX B 2005 |
Chain | Residue |
B | HOH2019 |
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 | SER319-PRO325 |