Structure of PDB 2glx Chain D Binding Site BS02

Receptor Information
>2glx Chain D (length=332) Species: 106592 (Ensifer adhaerens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NRWGLIGASTIAREWVIGAIRATGGEVVSMMSTSAERGAAYATENGIGKS
VTSVEELVGDPDVDAVYVSTTNELHREQTLAAIRAGKHVLCEKPLAMTLE
DAREMVVAAREAGVVLGTNHHLRNAAAHRAMRDAIAEGRIGRPIAARVFH
AVYLPPHLQGWRLERPEAGGGVILDITVHDADTLRFVLNDDPAEAVAISH
SAGMGKEGVEDGVMGVLRFQSGVIAQFHDAFTTKFAETGFEVHGTEGSLI
GRNVMTQKPVGTVTLRNAEGESQLPLDPANLYETALAAFHSAIEGHGQPS
ATGEDGVWSLATGLAVVKAAATGQAAEIETGL
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 chain2glx Chain D Residue 4500 [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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PDB2glx Crystal Structure of NADP(H)-Dependent 1,5-Anhydro-d-fructose Reductase from Sinorhizobium morelense at 2.2 A Resolution: Construction of a NADH-Accepting Mutant and Its Application in Rare Sugar Synthesis
Resolution2.2 Å
Binding residue
(original residue number in PDB)		G8 A9 S10 T11 I12 S33 T34 R38 S70 T71 N73 H76 E93 K94 N120 W162 R163 Q258 Y283
Binding residue
(residue number reindexed from 1)		G7 A8 S9 T10 I11 S32 T33 R37 S69 T70 N72 H75 E92 K93 N119 W161 R162 Q257 Y282
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) K94 H180
Catalytic site (residue number reindexed from 1) K93 H179
Enzyme Commision number 1.1.1.292: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming).
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0033712 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) activity

View graph for
Molecular Function
External links
PDB RCSB:2glx, PDBe:2glx, PDBj:2glx
PDBsum2glx
PubMed16906761
UniProtQ2I8V6|AFR_ENSAD 1,5-anhydro-D-fructose reductase (Gene Name=afr)

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