5JLA
Crystal Structure of Ribose-5-phosphate Isomerase from Brucella melitensis 16M
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | GLY16 |
| A | GLY63 |
| A | CYS88 |
| A | ALA89 |
| A | GLY90 |
| A | ILE112 |
| A | ILE139 |
| A | ALA140 |
| A | SER141 |
| A | TYR153 |
| A | LYS157 |
| A | SER19 |
| A | PRO183 |
| A | GLY184 |
| A | PHE185 |
| A | THR186 |
| A | THR188 |
| A | PRO189 |
| A | ALA190 |
| A | HOH590 |
| A | HOH597 |
| A | HOH601 |
| A | GLY20 |
| A | ILE21 |
| A | ASP40 |
| A | ARG41 |
| A | LEU60 |
| A | ASP61 |
| A | VAL62 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | GLY16 |
| B | SER19 |
| B | GLY20 |
| B | ILE21 |
| B | ASP40 |
| B | ARG41 |
| B | LEU60 |
| B | ASP61 |
| B | VAL62 |
| B | GLY63 |
| B | CYS88 |
| B | GLY90 |
| B | ILE112 |
| B | ILE139 |
| B | ALA140 |
| B | SER141 |
| B | TYR153 |
| B | LYS157 |
| B | PRO183 |
| B | GLY184 |
| B | PHE185 |
| B | THR186 |
| B | THR188 |
| B | PRO189 |
| B | ALA190 |
| B | ARG193 |
| B | HOH503 |
| B | HOH509 |
| B | HOH577 |
| B | HOH605 |
| B | HOH624 |
| B | HOH644 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue NAD C 401 |
| Chain | Residue |
| C | GLY16 |
| C | SER19 |
| C | GLY20 |
| C | ILE21 |
| C | ASP40 |
| C | ARG41 |
| C | LEU60 |
| C | ASP61 |
| C | VAL62 |
| C | GLY63 |
| C | CYS88 |
| C | GLY90 |
| C | ILE112 |
| C | ILE139 |
| C | ALA140 |
| C | SER141 |
| C | TYR153 |
| C | LYS157 |
| C | PRO183 |
| C | GLY184 |
| C | PHE185 |
| C | THR186 |
| C | THR188 |
| C | PRO189 |
| C | ALA190 |
| C | HOH562 |
| C | HOH591 |
| C | HOH624 |
| C | HOH650 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | binding site for residue NAD D 401 |
| Chain | Residue |
| D | CYS88 |
| D | ALA89 |
| D | GLY90 |
| D | ILE112 |
| D | ILE139 |
| D | ALA140 |
| D | SER141 |
| D | TYR153 |
| D | LYS157 |
| D | PRO183 |
| D | GLY184 |
| D | PHE185 |
| D | THR186 |
| D | THR188 |
| D | PRO189 |
| D | ALA190 |
| D | HOH535 |
| D | HOH585 |
| D | HOH608 |
| D | GLY16 |
| D | SER19 |
| D | GLY20 |
| D | ILE21 |
| D | ASP40 |
| D | ARG41 |
| D | LEU60 |
| D | ASP61 |
| D | VAL62 |
