Structure of PDB 7mj1 Chain C Binding Site BS02

Receptor Information
>7mj1 Chain C (length=200) Species: 220668 (Lactiplantibacillus plantarum WCFS1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NGFPEVIYGAGKTATQIVGIVQALSQQTLPILTTRLSAEKFAALQPALPT
AVYHATAQCMTVGEPAPKTPGYIAVVTAGTSDQPVAEEAAVTAETFGNRV
ERVYDVGVAGIHRLFAKLDVIRGARVVIVIAGMEGALASVVGGLVDKPVI
AVPTSVGYGTSFQGMTALLTMLNSCASGITVVNIDNGFGAAYSASMVNQM
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 chain7mj1 Chain C Residue 302 [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]
PDB7mj1 The LarB carboxylase/hydrolase forms a transient cysteinyl-pyridine intermediate during nickel-pincer nucleotide cofactor biosynthesis.
Resolution3.402 Å
Binding residue
(original residue number in PDB)		A124 T126 S127 D128 G153 V154 A177 G178 M179 E180 A182 L183 Y204
Binding residue
(residue number reindexed from 1)		A78 T80 S81 D82 G107 V108 A131 G132 M133 E134 A136 L137 Y158
Annotation score4
Enzymatic activity
Enzyme Commision number 2.5.1.143: pyridinium-3,5-biscarboxylic acid mononucleotide synthase.
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006189 'de novo' IMP biosynthetic process
Cellular Component
GO:0005886 plasma membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7mj1, PDBe:7mj1, PDBj:7mj1
PDBsum7mj1
PubMed34548397
UniProtF9UST0|LARB_LACPL Pyridinium-3,5-biscarboxylic acid mononucleotide synthase (Gene Name=larB)

[Back to BioLiP]