4M0K
Crystal structure of adenine phosphoribosyltransferase from Rhodothermus marinus DSM 4252, NYSGRC Target 029775.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002055 | molecular_function | adenine binding |
| A | 0003999 | molecular_function | adenine phosphoribosyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0006168 | biological_process | adenine salvage |
| A | 0016208 | molecular_function | AMP binding |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0044209 | biological_process | AMP salvage |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0002055 | molecular_function | adenine binding |
| B | 0003999 | molecular_function | adenine phosphoribosyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006166 | biological_process | purine ribonucleoside salvage |
| B | 0006168 | biological_process | adenine salvage |
| B | 0016208 | molecular_function | AMP binding |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0044209 | biological_process | AMP salvage |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0002055 | molecular_function | adenine binding |
| C | 0003999 | molecular_function | adenine phosphoribosyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006166 | biological_process | purine ribonucleoside salvage |
| C | 0006168 | biological_process | adenine salvage |
| C | 0016208 | molecular_function | AMP binding |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0044209 | biological_process | AMP salvage |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0002055 | molecular_function | adenine binding |
| D | 0003999 | molecular_function | adenine phosphoribosyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006166 | biological_process | purine ribonucleoside salvage |
| D | 0006168 | biological_process | adenine salvage |
| D | 0016208 | molecular_function | AMP binding |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0044209 | biological_process | AMP salvage |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE AMP A 300 |
| Chain | Residue |
| A | GLN25 |
| A | GLY130 |
| A | GLY131 |
| A | THR132 |
| A | LEU156 |
| A | HOH415 |
| A | HOH421 |
| A | HOH426 |
| A | HOH427 |
| A | HOH444 |
| A | HOH490 |
| A | PHE26 |
| A | HOH555 |
| A | LYS27 |
| A | GLU62 |
| A | ASP124 |
| A | ASP125 |
| A | VAL126 |
| A | ALA128 |
| A | THR129 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 301 |
| Chain | Residue |
| A | ASP77 |
| A | HOH472 |
| A | HOH474 |
| A | HOH521 |
| A | HOH522 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE AMP B 300 |
| Chain | Residue |
| B | GLN25 |
| B | PHE26 |
| B | LYS27 |
| B | ASP124 |
| B | ASP125 |
| B | VAL126 |
| B | ALA128 |
| B | THR129 |
| B | GLY130 |
| B | GLY131 |
| B | THR132 |
| B | LEU156 |
| B | HOH402 |
| B | HOH407 |
| B | HOH416 |
| B | HOH417 |
| B | HOH451 |
| B | HOH480 |
| B | HOH488 |
| B | HOH490 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 301 |
| Chain | Residue |
| B | HOH456 |
| B | HOH466 |
| B | HOH478 |
| B | HOH495 |
| B | HOH544 |
| B | HOH548 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE AMP C 201 |
| Chain | Residue |
| C | GLN25 |
| C | PHE26 |
| C | LYS27 |
| C | ASP124 |
| C | ASP125 |
| C | VAL126 |
| C | ALA128 |
| C | THR129 |
| C | GLY130 |
| C | GLY131 |
| C | THR132 |
| C | LEU156 |
| C | HOH303 |
| C | HOH311 |
| C | HOH315 |
| C | HOH316 |
| C | HOH391 |
| C | HOH398 |
| C | HOH404 |
| C | HOH469 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 202 |
| Chain | Residue |
| B | GLN11 |
| B | HOH409 |
| B | HOH437 |
| C | GLU134 |
| C | HOH331 |
| C | HOH368 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE AMP D 300 |
| Chain | Residue |
| D | GLN25 |
| D | PHE26 |
| D | LYS27 |
| D | ASP124 |
| D | ASP125 |
| D | VAL126 |
| D | ALA128 |
| D | THR129 |
| D | GLY130 |
| D | GLY131 |
| D | THR132 |
| D | LEU156 |
| D | HOH412 |
| D | HOH419 |
| D | HOH440 |
| D | HOH475 |
| D | HOH482 |
| D | HOH489 |
| D | HOH503 |
| D | HOH529 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 301 |
| Chain | Residue |
| D | HOH427 |
| D | HOH464 |
| D | HOH496 |
| D | HOH498 |
| A | GLU134 |
| D | GLN11 |
