Structure of PDB 5br4 Chain B Binding Site BS02

Receptor Information
>5br4 Chain B (length=384) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKV
TDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIAIGGGSPQ
DTCKAIGIISNNPEFADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTIN
YVITDEEKRRKFVCVDPHDIPQVAFIDADMMDGCPPALKAATGVDALTHA
IEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAGEEMALGQYVAG
MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYR
DIARVMGVKVEGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIP
ALAQAALDDVCTGGNPREATLEDIVELYHTAWLE
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 chain5br4 Chain B Residue 402 [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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PDB5br4 Mutations in adenine-binding pockets enhance catalytic properties of NAD(P)H-dependent enzymes.
Resolution0.91 Å
Binding residue
(original residue number in PDB)		D39 T41 L42 G97 G98 S99 D102 T140 T141 T144 T149 N151 V153 K162 C185 L189 H277
Binding residue
(residue number reindexed from 1)		D38 T40 L41 G96 G97 S98 D101 T139 T140 T143 T148 N150 V152 K161 C184 L188 H276
Annotation score4
Enzymatic activity
Enzyme Commision number 1.1.1.77: lactaldehyde reductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0008198 ferrous iron binding
GO:0008912 lactaldehyde reductase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0052660 R-lactaldehyde reductase activity
GO:0052661 S-lactaldehyde reductase activity
Biological Process
GO:0006004 fucose metabolic process
GO:0019301 rhamnose catabolic process
GO:0019317 fucose catabolic process
GO:0042355 L-fucose catabolic process
GO:0042846 glycol catabolic process
GO:0051143 propanediol metabolic process
Cellular Component
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:5br4, PDBe:5br4, PDBj:5br4
PDBsum5br4
PubMed26512129
UniProtP0A9S1|FUCO_ECOLI Lactaldehyde reductase (Gene Name=fucO)

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