Structure of PDB 3p2o Chain B Binding Site BS01

Receptor Information
>3p2o Chain B (length=282) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AMTLLDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVK
SKAKACEECGIKSLVYHLNENITQNELLALINTLNHDDSVHGILVQLPLP
DHICKDLILESIISSKDVDGFHPINVGYLNLGLESGFLPCTPLGVMKLLK
AYEIDLEGKDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTR
QADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVGDVDFEEVSK
KSSYITPVPGGVGPMTIAMLLENTVKSAKNRL
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 chain3p2o Chain B Residue 291 [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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PDB3p2o Crystal Structure of FolD Bifunctional Protein from
Resolution2.227 Å
Binding residue
(original residue number in PDB)		Y47 G164 A165 S166 V169 H188 I189 A207 A208 L213 V228 I230
Binding residue
(residue number reindexed from 1)		Y48 G165 A166 S167 V170 H189 I190 A208 A209 L214 V229 I231
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) S44 K51 Q95 D118
Catalytic site (residue number reindexed from 1) S45 K52 Q96 D119
Enzyme Commision number 1.5.1.5: methylenetetrahydrofolate dehydrogenase (NADP(+)).
3.5.4.9: methenyltetrahydrofolate cyclohydrolase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004477 methenyltetrahydrofolate cyclohydrolase activity
GO:0004488 methylenetetrahydrofolate dehydrogenase (NADP+) activity
GO:0016491 oxidoreductase activity
GO:0016787 hydrolase activity
Biological Process
GO:0000105 L-histidine biosynthetic process
GO:0006164 purine nucleotide biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0009086 methionine biosynthetic process
GO:0035999 tetrahydrofolate interconversion
Cellular Component
GO:0005829 cytosol

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Biological Process
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Cellular Component
External links
PDB RCSB:3p2o, PDBe:3p2o, PDBj:3p2o
PDBsum3p2o
PubMed
UniProtQ0PA35|FOLD_CAMJE Bifunctional protein FolD (Gene Name=folD)

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