Structure of PDB 1h6d Chain E Binding Site BS01

Receptor Information
>1h6d Chain E (length=382) Species: 542 (Zymomonas mobilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AATLPAGASQVPTTPAGRPMPYAIRPMPEDRRFGYAIVGLGKYALNQILP
GFAGCQHSRIEALVSGNAEKAKIVAAEYGVDPRKIYDYSNFDKIAKDPKI
DAVYIILPNSLHAEFAIRAFKAGKHVMCEKPMATSVADCQRMIDAAKAAN
KKLMIGYRCHYDPMNRAAVKLIRENQLGKLGMVTTDNSDVMDQNDPAQQW
RLRRELAGGGSLMDIGIYGLNGTRYLLGEEPIEVRAYTYSDPNDERFVEV
EDRIIWQMRFRSGALSHGASSYSTTTTSRFSVQGDKAVLLMDPATGYYQN
LISVQTPGHANQSMMPQFIMPANNQFSAQLDHLAEAVINNKPVRSPGEEG
MQDVRLIQAIYEAARTGRPVNTDWGYVRQGGY
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 chain1h6d Chain E Residue 500 [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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PDB1h6d Crystal Structures of the Precursor Form of Glucose-Fructose Oxidoreductase from Zymomonas Mobilis and its Complexes with Bound Ligands
Resolution2.05 Å
Binding residue
(original residue number in PDB)		G90 L91 G92 K93 Y94 S116 G117 K121 Y139 I157 L158 P159 N160 H163 E180 K181 R209 A248 W251 R252 Y269 Y348
Binding residue
(residue number reindexed from 1)		G39 L40 G41 K42 Y43 S65 G66 K70 Y88 I106 L107 P108 N109 H112 E129 K130 R158 A197 W200 R201 Y218 Y297
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K181 Y269
Catalytic site (residue number reindexed from 1) K130 Y218
Enzyme Commision number 1.1.99.28: glucose-fructose oxidoreductase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding

View graph for
Molecular Function
External links
PDB RCSB:1h6d, PDBe:1h6d, PDBj:1h6d
PDBsum1h6d
PubMed11705375
UniProtQ07982|GFO_ZYMMO Glucose--fructose oxidoreductase (Gene Name=gfo)

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