Structure of PDB 1rye Chain C Binding Site BS01

Receptor Information
>1rye Chain C (length=339) Species: 542 (Zymomonas mobilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RRFGYAIVGLGKYALNQILPGFAGCQHSRIEALVSGNAEKAKIVAAEYGV
DPRKIYDYSNFDKIAKDPKIDAVYIILPNSLHAEFAIRAFKAGKHVMCEK
PMATSVADCQRMIDAAKAANKKLMIGYRCHYDPMNRAAVKLIRENQLGKL
GMVTTDNSDVMDQNDPAQQWRLRRELAGGGSLMDIGIYGLNGTRYLLGEE
PIEVRAYTYSDPNDERFVEVEDRIIWQMRFRSGALSHGASSYSTTTTSRF
SVQGDKAVLLMDPATGYYQNLISVQTPPANNQFSAQLDHLAEAVINNKPV
RSPGEEGMQDVRLIQAIYEAARTGRPVNTDWGYVRQGGY
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 chain1rye Chain C Residue 502 [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]
PDB1rye Crystal Structure of the Shifted Form of the Glucose-Fructose Oxidoreductase from Zymomonas mobilis
Resolution2.3 Å
Binding residue
(original residue number in PDB)		G38 L39 G40 K41 Y42 S64 G65 K69 Y87 I105 L106 P107 H111 E128 K129 R157 A196 W199 R200 Y217 Y296
Binding residue
(residue number reindexed from 1)		G9 L10 G11 K12 Y13 S35 G36 K40 Y58 I76 L77 P78 H82 E99 K100 R128 A167 W170 R171 Y188 Y267
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K129 Y217
Catalytic site (residue number reindexed from 1) K100 Y188
Enzyme Commision number 1.1.99.28: glucose-fructose oxidoreductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0047061 glucose-fructose oxidoreductase activity
Biological Process
GO:0006061 sorbitol biosynthetic process
Cellular Component
GO:0042597 periplasmic space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1rye, PDBe:1rye, PDBj:1rye
PDBsum1rye
PubMed
UniProtQ07982|GFO_ZYMMO Glucose--fructose oxidoreductase (Gene Name=gfo)

[Back to BioLiP]