Structure of PDB 6wpr Chain B Binding Site BS01

Receptor Information
>6wpr Chain B (length=235) Species: 470 (Acinetobacter baumannii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RKVALVTGASRGIGAAIAQQLIQDGYFVVGTATSESGAQKLTDSFGEQGA
GLALDVRNLDEIEAVVSHIEQNYGPVLVLVNNAGITKDNLLLRMSEDDWD
DILNIHLKAVYRLSKRVLKGMTKARFGRIINISSVVAHFANPGQANYSAA
KAGIEAFSRSLAKEMGSRQITVNSVAPGFIATESEDIRKKMSDQVALNRL
GEPQDIANAVSFLASDKAGYITGTVLHVNGGLYMA
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 chain6wpr Chain B Residue 301 [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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PDB6wpr Insights into Acinetobacter baumannii fatty acid synthesis 3-oxoacyl-ACP reductases.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		G12 S14 T37 D59 V60 N86 A87 G88 I89 I136 Y151
Binding residue
(residue number reindexed from 1)		G8 S10 T33 D55 V56 N82 A83 G84 I85 I132 Y147
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) G16 S138 Y151
Catalytic site (residue number reindexed from 1) G12 S134 Y147
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004316 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0051287 NAD binding
Biological Process
GO:0006633 fatty acid biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6wpr, PDBe:6wpr, PDBj:6wpr
PDBsum6wpr
PubMed33782435
UniProtV5VHN7

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