Structure of PDB 1onp Chain A

Receptor sequence

>1onpA (length=397) Species: 562 (Escherichia coli)

MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFS
PRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAA
IVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVD
SEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLAT
MTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLI
HPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFC
KLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQ
IRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLA

3D structure

• PDB: 1onp 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

Enzymatic activity

• Enzyme Commision number: 1.1.1.267: 1-deoxy-D-xylulose-5-phosphate reductoisomerase.

Interaction with ligand

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 E231
BS02	FOM	A	E152 S186 W212 N227 K228	E152 S186 W212 N227 K228	PDBbind-CN: -logKd/Ki=7.52,IC50=0.030uM BindingDB: IC50=30nM

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0030145 manganese ion binding
• GO:0030604 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding
• GO:0070402 NADPH binding

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

Cellular Component

• GO:1990065 Dxr protein complex

External links

• PDB: RCSB:1onp, PDBe:1onp, PDBj:1onp
• PDBsum: 1onp
• PubMed: 12621040
• UniProt: P45568|DXR_ECOLI 1-deoxy-D-xylulose 5-phosphate reductoisomerase (Gene Name=dxr)