Structure of PDB 1drw Chain A Binding Site BS01

Receptor Information
>1drw Chain A (length=272) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGE
LAGAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVI
GTTGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYT
DIEIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGER
VPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSA
LWLSGKESGLFDMRDVLDLNNL
Ligand information
Ligand IDNHD
InChIInChI=1S/C21H26N6O15P2/c22-17(32)9-2-1-3-26(4-9)20-15(30)13(28)10(40-20)5-38-43(34,35)42-44(36,37)39-6-11-14(29)16(31)21(41-11)27-8-25-12-18(27)23-7-24-19(12)33/h1-4,7-8,10-11,13-16,20-21,28-31H,5-6H2,(H4-,22,23,24,32,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyDGVSIBCCYUVRNA-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(O)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)n4cnc5c4ncnc5O)O)O)O)O)C(=O)N
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)n4cnc5c4ncnc5O)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(O)ncnc45)[CH](O)[CH]2O
FormulaC21 H26 N6 O15 P2
NameNICOTINAMIDE PURIN-6-OL-DINUCLEOTIDE
ChEMBL
DrugBank
ZINC
PDB chain1drw Chain A 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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PDB1drw Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		G12 G15 R16 M17 E38 R39 F79 T80 R81 G102 T103 T104 A127 N128 F129 F243
Binding residue
(residue number reindexed from 1)		G11 G14 R15 M16 E37 R38 F78 T79 R80 G101 T102 T103 A126 N127 F128 F242
Annotation score3
Binding affinityMOAD: Kd=1.48uM
Enzymatic activity
Catalytic site (original residue number in PDB) H159 K163
Catalytic site (residue number reindexed from 1) H158 K162
Enzyme Commision number 1.17.1.8: 4-hydroxy-tetrahydrodipicolinate reductase.
Gene Ontology
Molecular Function
GO:0008839 4-hydroxy-tetrahydrodipicolinate reductase
GO:0016491 oxidoreductase activity
GO:0016726 oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
GO:0042802 identical protein binding
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0019877 diaminopimelate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1drw, PDBe:1drw, PDBj:1drw
PDBsum1drw
PubMed8873595
UniProtP04036|DAPB_ECOLI 4-hydroxy-tetrahydrodipicolinate reductase (Gene Name=dapB)

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