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 | 36 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00183 |
Chain | Residue | Details |
A | THR12 | |
A | SER143 | |
A | GLU144 | |
A | SER164 | |
A | HIS187 | |
A | GLY193 | |
A | SER200 | |
A | ASN205 | |
A | LYS206 | |
A | GLU209 | |
B | THR12 | |
A | GLY13 | |
B | GLY13 | |
B | SER14 | |
B | ILE15 | |
B | ASN39 | |
B | ASN116 | |
B | LYS117 | |
B | GLU118 | |
B | ASP142 | |
B | SER143 | |
B | GLU144 | |
A | SER14 | |
B | SER164 | |
B | HIS187 | |
B | GLY193 | |
B | SER200 | |
B | ASN205 | |
B | LYS206 | |
B | GLU209 | |
A | ILE15 | |
A | ASN39 | |
A | ASN116 | |
A | LYS117 | |
A | GLU118 | |
A | ASP142 |