4A03
Crystal Structure of Mycobacterium tuberculosis DXR in complex with the antibiotic FR900098 and cofactor NADPH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
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 | 0050897 | molecular_function | cobalt ion binding |
A | 0051483 | biological_process | terpenoid biosynthetic process, mevalonate-independent |
A | 0051484 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
A | 0070402 | molecular_function | NADPH binding |
B | 0000287 | molecular_function | magnesium ion 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 | 0050897 | molecular_function | cobalt ion binding |
B | 0051483 | biological_process | terpenoid biosynthetic process, mevalonate-independent |
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 | 5 |
Details | BINDING SITE FOR RESIDUE MN A 401 |
Chain | Residue |
A | LYS128 |
A | ASP151 |
A | GLU153 |
A | GLU222 |
A | F98501 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE F98 A 501 |
Chain | Residue |
A | ALA176 |
A | SER177 |
A | HIS200 |
A | TRP203 |
A | MET205 |
A | ASN209 |
A | SER213 |
A | ASN218 |
A | LYS219 |
A | GLU222 |
A | MN401 |
A | NDP601 |
A | HOH2143 |
A | HOH2144 |
A | HOH2185 |
A | LYS128 |
A | ASP151 |
A | SER152 |
A | GLU153 |
site_id | AC3 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE NDP A 601 |
Chain | Residue |
A | GLY19 |
A | SER20 |
A | THR21 |
A | GLY22 |
A | SER23 |
A | ILE24 |
A | ALA46 |
A | GLY47 |
A | GLY48 |
A | ALA49 |
A | HIS50 |
A | ALA69 |
A | ALA103 |
A | LEU104 |
A | LEU108 |
A | ALA126 |
A | ASN127 |
A | LYS128 |
A | GLU129 |
A | ASP151 |
A | MET205 |
A | GLY206 |
A | ASN209 |
A | MET267 |
A | F98501 |
A | HOH2003 |
A | HOH2008 |
A | HOH2030 |
A | HOH2035 |
A | HOH2074 |
A | HOH2114 |
A | HOH2178 |
A | HOH2179 |
A | HOH2296 |
A | HOH2297 |
A | HOH2298 |
A | HOH2299 |
A | HOH2300 |
A | HOH2301 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 701 |
Chain | Residue |
A | THR64 |
A | ASN65 |
A | PRO81 |
A | TYR82 |
A | LYS171 |
A | ASP235 |
A | ILE237 |
A | ASP238 |
A | ARG313 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 401 |
Chain | Residue |
B | LYS128 |
B | ASP151 |
B | GLU153 |
B | GLU222 |
B | F98501 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE F98 B 501 |
Chain | Residue |
B | LYS128 |
B | ASP151 |
B | SER152 |
B | GLU153 |
B | ALA176 |
B | SER177 |
B | HIS200 |
B | TRP203 |
B | MET205 |
B | ASN209 |
B | SER213 |
B | ASN218 |
B | LYS219 |
B | GLU222 |
B | MN401 |
B | NDP601 |
B | HOH2105 |
B | HOH2106 |
B | HOH2148 |
site_id | AC7 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NDP B 601 |
Chain | Residue |
B | SER23 |
B | ILE24 |
B | ALA46 |
B | GLY47 |
B | GLY48 |
B | ALA49 |
B | HIS50 |
B | ALA69 |
B | ALA103 |
B | LEU104 |
B | LEU108 |
B | ALA126 |
B | ASN127 |
B | LYS128 |
B | GLU129 |
B | ASP151 |
B | MET205 |
B | GLY206 |
B | ASN209 |
B | MET267 |
B | F98501 |
B | HOH2001 |
B | HOH2006 |
B | HOH2007 |
B | HOH2024 |
B | HOH2046 |
B | HOH2078 |
B | HOH2142 |
B | HOH2143 |
B | HOH2227 |
B | GLY19 |
B | THR21 |
B | GLY22 |
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 | THR21 | |
A | SER152 | |
A | GLU153 | |
A | SER177 | |
A | HIS200 | |
A | GLY206 | |
A | SER213 | |
A | ASN218 | |
A | LYS219 | |
A | GLU222 | |
B | THR21 | |
A | GLY22 | |
B | GLY22 | |
B | SER23 | |
B | ILE24 | |
B | GLY47 | |
B | ASN127 | |
B | LYS128 | |
B | GLU129 | |
B | ASP151 | |
B | SER152 | |
B | GLU153 | |
A | SER23 | |
B | SER177 | |
B | HIS200 | |
B | GLY206 | |
B | SER213 | |
B | ASN218 | |
B | LYS219 | |
B | GLU222 | |
A | ILE24 | |
A | GLY47 | |
A | ASN127 | |
A | LYS128 | |
A | GLU129 | |
A | ASP151 |