6O55
Crystal Structure of N5-carboxyaminoimidazole ribonucleotide mutase (PurE) from Legionella pneumophila
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0034023 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide mutase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0034023 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide mutase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0034023 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide mutase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0006164 | biological_process | purine nucleotide biosynthetic process |
| D | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0034023 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide mutase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 201 |
| Chain | Residue |
| A | MET90 |
| A | GLY118 |
| A | LYS119 |
| A | HOH358 |
| A | HOH367 |
| D | GLN92 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 202 |
| Chain | Residue |
| A | HOH401 |
| B | MET90 |
| B | GLY118 |
| B | LYS119 |
| B | HOH373 |
| B | HOH406 |
| A | GLN92 |
| A | THR93 |
| A | HOH305 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 203 |
| Chain | Residue |
| A | THR43 |
| A | ASP45 |
| A | LYS46 |
| A | HOH317 |
| A | HOH402 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 201 |
| Chain | Residue |
| A | ASN95 |
| B | ASN95 |
| B | HOH316 |
| C | ASN95 |
| C | HOH318 |
| C | HOH406 |
| D | ASN95 |
| D | EDO201 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 203 |
| Chain | Residue |
| B | THR43 |
| B | ASP45 |
| B | LYS46 |
| B | HOH334 |
| B | HOH371 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 C 201 |
| Chain | Residue |
| C | LEU94 |
| C | ASN95 |
| C | HOH318 |
| D | EDO201 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CL C 202 |
| Chain | Residue |
| C | THR43 |
| C | PRO44 |
| C | ASP45 |
| C | LYS46 |
| C | HOH395 |
| C | HOH401 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 201 |
| Chain | Residue |
| A | ASN95 |
| B | EDO201 |
| C | PG4201 |
| D | ASN95 |
| D | EDO202 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue EDO D 202 |
| Chain | Residue |
| D | EDO201 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue CL D 203 |
| Chain | Residue |
| D | THR43 |
| D | ASP45 |
| D | LYS46 |
| D | HOH412 |
| D | HOH445 |
