Structure of PDB 1ono Chain A |
>1onoA (length=389) Species: 562 (Escherichia coli) [Search protein sequence] |
MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFS PRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAA IVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVD SEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLAT MTPDQACRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHS MVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFA APDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAA LNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLA |
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PDB | 1ono Structural basis of fosmidomycin action revealed by the complex with 2-C-methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the catalytic mechanism and anti-malaria drug development. |
Chain | A |
Resolution | 2.5 Å |
3D structure |
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Enzyme Commision number |
1.1.1.267: 1-deoxy-D-xylulose-5-phosphate reductoisomerase. |
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Site # |
Ligand |
Ligand chain |
Binding residues on receptor (original residue number in PDB) |
Binding residues on receptor (residue number reindexed from 1) |
Binding affinity |
BS01 |
MN |
A |
D150 E152 E231 |
D150 E152 E223 |
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Biological Process |
GO:0008299 |
isoprenoid biosynthetic process |
GO:0019288 |
isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
GO:0051484 |
isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process |
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