5LXE
F420-dependent glucose-6-phosphate dehydrogenase from Rhodococcus jostii RHA1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0052749 | molecular_function | glucose-6-phosphate dehydrogenase (coenzyme F420) activity |
| A | 0070967 | molecular_function | coenzyme F420 binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0052749 | molecular_function | glucose-6-phosphate dehydrogenase (coenzyme F420) activity |
| B | 0070967 | molecular_function | coenzyme F420 binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | ARG318 |
| A | GLU321 |
| A | ARG325 |
| A | HOH524 |
| B | PRO329 |
| B | ARG332 |
| B | HOH544 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| A | ARG186 |
| B | THR236 |
| B | ARG318 |
| B | ARG325 |
| B | HOH522 |
| B | HOH582 |
| B | HOH657 |
| A | ARG132 |
| A | TYR183 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| A | THR236 |
| A | ARG318 |
| A | ARG325 |
| B | GLN324 |
| B | HOH502 |
| B | HOH544 |
| B | HOH585 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | LYS8 |
| B | SER10 |
| B | ALA11 |
| B | GLU12 |
| B | SER37 |
| B | HIS39 |
| B | HIS310 |
| B | HOH511 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02123 |
| Chain | Residue | Details |
| A | HIS39 | |
| B | HIS39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02123 |
| Chain | Residue | Details |
| A | GLU108 | |
| B | GLU108 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02123 |
| Chain | Residue | Details |
| A | ASP38 | |
| A | ARG282 | |
| B | ASP38 | |
| B | THR75 | |
| B | THR106 | |
| B | ASN111 | |
| B | GLY176 | |
| B | VAL179 | |
| B | THR194 | |
| B | LYS197 | |
| B | LYS258 | |
| A | THR75 | |
| B | ARG282 | |
| A | THR106 | |
| A | ASN111 | |
| A | GLY176 | |
| A | VAL179 | |
| A | THR194 | |
| A | LYS197 | |
| A | LYS258 |
