Structure of PDB 1q0q Chain B Binding Site BS02

Receptor Information
>1q0q Chain B (length=398) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFS
PRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAA
IVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVD
SEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLAT
MTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLI
HPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFC
KLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQ
IRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS
Ligand information
Ligand IDNDP
InChIInChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyACFIXJIJDZMPPO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
FormulaC21 H30 N7 O17 P3
NameNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
ChEMBLCHEMBL407009
DrugBankDB02338
ZINCZINC000008215411
PDB chain1q0q Chain B Residue 2002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1q0q The crystal structure of E.coli 1-deoxy-D-xylulose-5-phosphate reductoisomerase in a ternary complex with the antimalarial compound fosmidomycin and NADPH reveals a tight-binding closed enzyme conformation.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G8 T10 G11 S12 I13 A35 G36 K37 N38 D57 A100 I101 V102 A123 N124 K125 E126 D150 M214 G215 I218
Binding residue
(residue number reindexed from 1)		G8 T10 G11 S12 I13 A35 G36 K37 N38 D57 A100 I101 V102 A123 N124 K125 E126 D150 M214 G215 I218
Annotation score4
Enzymatic activity
Enzyme Commision number 1.1.1.267: 1-deoxy-D-xylulose-5-phosphate reductoisomerase.
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1q0q, PDBe:1q0q, PDBj:1q0q
PDBsum1q0q
PubMed15567415
UniProtP45568|DXR_ECOLI 1-deoxy-D-xylulose 5-phosphate reductoisomerase (Gene Name=dxr)

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