Structure of PDB 5t79 Chain A Binding Site BS01

Receptor Information
>5t79 Chain A (length=315) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIYQPDENRYHTMEYRRCGRSGVKLPAISLGLWHNFGDTTRVENSRALLQ
RAFDLGITHFDLANNYGPPPGSAECNFGRILQEDFLPWRDELIISTKAGY
TMWDGPYGDWGSRKYLIASLDQSLKRMGLEYVDIFYHHRPDPETPLKETM
KALDHLVRHGKALYVGISNYPADLARQAIDILEDLGTPCLIHQPKYSLFE
RWVEDGLLALLQEKGVGSIAFSPLAGGQLTDRYLLKPEQITADKLEKVRR
LNELAARRGQKLSQMALAWVLRNDNVTSVLIGASKPSQIEDAVGMLANRR
FSAAECAEIDAILEG
Ligand information
Ligand IDNDP
InChIInChI=1S/C21H30N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1,3-4,7-8,10-11,13-16,20-21,29-31H,2,5-6H2,(H2,23,32)(H,36,37)(H,38,39)(H2,22,24,25)(H2,33,34,35)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyACFIXJIJDZMPPO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)OP(=O)(O)O)N
FormulaC21 H30 N7 O17 P3
NameNADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
ChEMBLCHEMBL407009
DrugBankDB02338
ZINCZINC000008215411
PDB chain5t79 Chain A Residue 404 [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]
PDB5t79 Structural and biochemical studies of novel aldo-keto reductases for the biocatalytic conversion of 3-hydroxybutanal to 1,3-butanediol.
Resolution1.86 Å
Binding residue
(original residue number in PDB)		G31 W33 Y66 H138 N169 Q193 F221 S222 L224 G226 T230 R232 S278 L295 G297 S299 Q303
Binding residue
(residue number reindexed from 1)		G31 W33 Y66 H138 N169 Q193 F221 S222 L224 G226 T230 R232 S263 L280 G282 S284 Q288
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0051596 methylglyoxal catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5t79, PDBe:5t79, PDBj:5t79
PDBsum5t79
PubMed28130301
UniProtQ8ZNA1

[Back to BioLiP]