3A14
Crystal structure of DXR from Thermotoga maritima, in complex with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030604 | molecular_function | 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
| B | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NDP A 3003 |
| Chain | Residue |
| A | LYS24 |
| A | ILE29 |
| A | ARG30 |
| A | LEU31 |
| A | PHE50 |
| B | LYS45 |
| B | LYS48 |
| B | GLU49 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP A 3001 |
| Chain | Residue |
| A | THR12 |
| A | GLY13 |
| A | SER14 |
| A | ILE15 |
| A | HIS37 |
| A | SER38 |
| A | ASN39 |
| A | THR58 |
| A | ALA92 |
| A | VAL93 |
| A | SER94 |
| A | SER97 |
| A | ALA115 |
| A | ASN116 |
| A | LYS117 |
| A | GLU118 |
| A | ASP142 |
| A | ILE196 |
| A | HOH409 |
| A | HOH431 |
| A | HOH433 |
| A | HOH441 |
| A | HOH501 |
| A | GLY10 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 900 |
| Chain | Residue |
| A | ASP142 |
| A | GLU144 |
| A | GLU209 |
| A | HOH500 |
| A | HOH501 |
| A | HOH502 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NDP B 3002 |
| Chain | Residue |
| B | GLY10 |
| B | THR12 |
| B | GLY13 |
| B | SER14 |
| B | ILE15 |
| B | HIS37 |
| B | SER38 |
| B | ASN39 |
| B | THR58 |
| B | ALA92 |
| B | VAL93 |
| B | SER94 |
| B | SER97 |
| B | ALA115 |
| B | ASN116 |
| B | LYS117 |
| B | GLU118 |
| B | ASP142 |
| B | HOH407 |
| B | HOH465 |
| B | HOH471 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD A 800 |
| Chain | Residue |
| A | ALA163 |
| A | SER164 |
| A | ASP199 |
| A | SER200 |
| A | MET203 |
| A | ASN205 |
| A | LYS206 |
| A | HOH499 |
| A | HOH500 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 901 |
| Chain | Residue |
| B | ASP142 |
| B | GLU144 |
| B | GLU209 |
| B | HOH600 |
| B | HOH601 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 801 |
| Chain | Residue |
| B | ALA163 |
| B | SER164 |
| B | SER200 |
| B | ASN205 |
| B | LYS206 |
| B | HOH390 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 33 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00183","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
