Structure of PDB 3wfj Chain H Binding Site BS01

Receptor Information
>3wfj Chain H (length=250) Species: 1352 (Enterococcus faecium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IAIAGAGAMGSRFGLMLHQVLLIDGWAEHVLIILFTKAMQLEKMLQEVLC
LLNGIGHEDIIEKFVPMENIYIGNTMWTAGLEGPGQVGSGSVELQNLGDG
KEAAAKKLADKLNAHFSDNIHYSIYRKACVNGTMNGLCTILDVNMAELGK
TSTAHKMVATIVNEFAKVAAVEKIELDVPEVIAHCESCFDPETIGLHYPS
MYQDLIKNHRLTEIDYINGAISRKGKKYGVATPYCDFLTELVHAKEDSLN
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain3wfj Chain H Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3wfj The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		G9 A10 M11 D30 W32 F77 T78 K79 Q82 L104 N105 W129 T130 A131 L133 R270 E273
Binding residue
(residue number reindexed from 1)		G7 A8 M9 D24 W26 F35 T36 K37 Q40 L52 N53 W77 T78 A79 L81 R210 E213
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) K187
Catalytic site (residue number reindexed from 1) K127
Enzyme Commision number 1.1.1.169: 2-dehydropantoate 2-reductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008677 2-dehydropantoate 2-reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0015940 pantothenate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3wfj, PDBe:3wfj, PDBj:3wfj
PDBsum3wfj
PubMed23954635
UniProtE3USM3

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