Structure of PDB 5wpj Chain A Binding Site BS01

Receptor Information
>5wpj Chain A (length=369) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ISWNGFSKKSYQERLELLKAQALLSPERQASLEKDEQMSVTVADQLSENV
VGTFSLPYSLVPEVLVNGQEYTVPYVTEEPSVVAAASYASKIIKRAGGFT
AQVHQRQMIGQVALYQVANPKLAQEKIASKKAELLELANQAYPSIVKRGG
GARDLHVEQIKGEPDFLVVYIHVDTQEAMGANMLNTMLEALKPVLEELSQ
GQSLMGILSNYATDSLVTASCRIAFRYLSRQKDQGREIAEKIALASQFAQ
ADPYRAATHNKGIFNGIDAILIATGNDWRAIEAGAHAFASRDGRYQGLSC
WTLDLEREELVGEMTLPMPVATKGGSIGLNPRVALSHDLLGNPSARELAQ
IIESIGLAQNFAALKALVS
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 chain5wpj Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5wpj Structural Features and Domain Movements Controlling Substrate Binding and Cofactor Specificity in Class II HMG-CoA Reductase.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		R150 T177 E179 A180 M181 G182 A183 N184 N212
Binding residue
(residue number reindexed from 1)		R148 T175 E177 A178 M179 G180 A181 N182 N210
Annotation score3
Enzymatic activity
Enzyme Commision number 1.1.1.88: hydroxymethylglutaryl-CoA reductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004420 hydroxymethylglutaryl-CoA reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0140643 hydroxymethylglutaryl-CoA reductase (NADH) activity
Biological Process
GO:0015936 coenzyme A metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5wpj, PDBe:5wpj, PDBj:5wpj
PDBsum5wpj
PubMed29224355
UniProtQ8DNS5

[Back to BioLiP]