5KS1
1-deoxy-D-xylulose 5-phosphate reductoisomerase from Vibrio vulnificus
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 | 4 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | GLN158 |
A | LEU160 |
B | GLN158 |
B | LEU160 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | GLU288 |
A | ARG289 |
B | SER175 |
B | GLY177 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | PRO148 |
A | VAL149 |
A | ASP150 |
A | HIS153 |
A | GLU234 |
A | LEU122 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PO4 A 504 |
Chain | Residue |
A | GLU152 |
A | GLY185 |
A | SER186 |
A | ASN227 |
A | LYS228 |
A | MN505 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue MN A 505 |
Chain | Residue |
A | GLU152 |
A | GLU231 |
A | PO4504 |
A | HOH652 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO B 501 |
Chain | Residue |
B | LEU122 |
B | ASN124 |
B | PRO148 |
B | VAL149 |
B | ASP150 |
B | HIS153 |
B | GLU234 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | SER151 |
B | HIS257 |
B | ASP275 |
B | PRO279 |
B | HOH639 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
A | VAL294 |
A | PRO296 |
B | SER179 |
B | TYR262 |
B | LEU263 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue PO4 B 504 |
Chain | Residue |
B | GLY185 |
B | SER186 |
B | SER222 |
B | ASN227 |
B | LYS228 |
B | HOH618 |
B | HOH630 |
B | HOH637 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue MN B 505 |
Chain | Residue |
B | GLU152 |
B | GLU231 |
B | HOH618 |
B | HOH620 |
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 | THR10 | |
A | SER151 | |
A | GLU152 | |
A | SER186 | |
A | HIS209 | |
A | GLY215 | |
A | SER222 | |
A | ASN227 | |
A | LYS228 | |
A | GLU231 | |
B | THR10 | |
A | GLY11 | |
B | GLY11 | |
B | SER12 | |
B | ILE13 | |
B | ASN38 | |
B | ASN124 | |
B | LYS125 | |
B | GLU126 | |
B | ASP150 | |
B | SER151 | |
B | GLU152 | |
A | SER12 | |
B | SER186 | |
B | HIS209 | |
B | GLY215 | |
B | SER222 | |
B | ASN227 | |
B | LYS228 | |
B | GLU231 | |
A | ILE13 | |
A | ASN38 | |
A | ASN124 | |
A | LYS125 | |
A | GLU126 | |
A | ASP150 |