5F3M
Crystal structure of dihydroneopterin aldolase from Bacillus anthracis complexed with L-neopterin at 1.5 Angstroms resolution .
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006760 | biological_process | folic acid-containing compound metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046656 | biological_process | folic acid biosynthetic process |
| B | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006760 | biological_process | folic acid-containing compound metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046656 | biological_process | folic acid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue NEU A 201 |
| Chain | Residue |
| A | VAL17 |
| A | VAL72 |
| A | GLU73 |
| A | LYS99 |
| A | PRO103 |
| A | HOH327 |
| A | HOH338 |
| A | PHE18 |
| A | GLU21 |
| A | LEU47 |
| A | SER50 |
| A | VAL51 |
| A | ASN52 |
| A | TYR53 |
| A | LEU71 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NI A 202 |
| Chain | Residue |
| A | HIS49 |
| A | HIS49 |
| A | HOH301 |
| A | HOH301 |
| A | HOH380 |
| A | HOH380 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 203 |
| Chain | Residue |
| A | THR68 |
| A | LYS70 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 204 |
| Chain | Residue |
| A | TYR5 |
| A | LYS96 |
| A | GLU114 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 205 |
| Chain | Residue |
| A | GLY42 |
| A | GLU43 |
| A | SER44 |
| A | ASP45 |
| A | TYR69 |
| A | SER74 |
| A | ASN78 |
| A | HOH336 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue NEU B 201 |
| Chain | Residue |
| B | VAL17 |
| B | PHE18 |
| B | GLU21 |
| B | LEU47 |
| B | SER50 |
| B | VAL51 |
| B | ASN52 |
| B | TYR53 |
| B | LEU71 |
| B | VAL72 |
| B | GLU73 |
| B | LYS99 |
| B | PRO103 |
| B | HOH328 |
| B | HOH331 |
| B | HOH379 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue NI B 202 |
| Chain | Residue |
| B | HIS49 |
| B | HIS49 |
| B | HOH370 |
| B | HOH370 |
| B | HOH378 |
| B | HOH378 |
| B | HOH381 |
| B | HOH381 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 203 |
| Chain | Residue |
| B | GLU65 |
| B | ASP66 |
| B | ARG67 |
| B | THR68 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 204 |
| Chain | Residue |
| B | TYR87 |
| B | GLU88 |
| B | SER89 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue FMT B 205 |
| Chain | Residue |
| B | TYR5 |
| B | LYS96 |
| B | GLU114 |
| B | HOH391 |
| B | HOH413 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 206 |
| Chain | Residue |
| A | HOH316 |
| A | HOH323 |
| B | GLN26 |
| B | ASP101 |
| B | PRO102 |
| B | PRO103 |
| B | HOH349 |
| B | HOH371 |
| B | HOH397 |
