3PBM
The crystal structure of adenosine deaminase in complex with chloropurine from Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000034 | molecular_function | adenine deaminase activity |
| A | 0006146 | biological_process | adenine catabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019239 | molecular_function | deaminase activity |
| A | 0043103 | biological_process | hypoxanthine salvage |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000034 | molecular_function | adenine deaminase activity |
| B | 0006146 | biological_process | adenine catabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019239 | molecular_function | deaminase activity |
| B | 0043103 | biological_process | hypoxanthine salvage |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 327 |
| Chain | Residue |
| A | HIS16 |
| A | HIS18 |
| A | HIS196 |
| A | ASP277 |
| A | ES4328 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ES4 A 328 |
| Chain | Residue |
| A | SER169 |
| A | HIS196 |
| A | GLU199 |
| A | HIS220 |
| A | ASP277 |
| A | ASP278 |
| A | ZN327 |
| A | HOH343 |
| A | HIS18 |
| A | LEU56 |
| A | LEU60 |
| A | TYR63 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 327 |
| Chain | Residue |
| B | HIS16 |
| B | HIS18 |
| B | HIS196 |
| B | ASP277 |
| B | ES4328 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ES4 B 328 |
| Chain | Residue |
| B | HIS18 |
| B | LEU56 |
| B | LEU60 |
| B | TYR63 |
| B | SER169 |
| B | HIS196 |
| B | GLU199 |
| B | HIS220 |
| B | ASP277 |
| B | ASP278 |
| B | ZN327 |
| B | HOH348 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2010","submissionDatabase":"PDB data bank","title":"The crystal structure of adenosine deaminase in complex with adenine, chloropurine and hypoxanthine from pseudomonas aeruginosa.","authoringGroup":["New York structural genomix research consortium (NYSGXRC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01962","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
