Structure of PDB 1evj Chain D Binding Site BS01

Receptor Information
>1evj Chain D (length=338) Species: 542 (Zymomonas mobilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RRFGYAIVGLGKYALNQILPGFAGCQHSRIEALVDGNAEKAKIVAAEYGV
DPRKIYDYSNFDKIAKDPKIDAVYIILPNSLHAEFAIRAFKAGKHVMCEK
PMATSVADCQRMIDAAKAANKKLMIGYRCHYDPMNRAAVKLIRENQLGKL
GMVTTDNSDVMDQNDPAQQWRLRRELAGGGSLMDIGIYGLNGTRYLLGEE
PIEVRAYTYSDPNDERFVEVEDRIIWQMRFRSGALSHGASSYSTTTTSRF
SVQGDKAVLLMDPATGYYQNLISVQTPGNNQFSAQLDHLAEAVINNKPVR
SPGEEGMQDVRLIQAIYEAARTGRPVNTDWGYVRQGGY
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 chain1evj Chain D Residue 503 [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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PDB1evj Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		L39 G40 K41 Y42 I105 L106 P107 H111 E128 K129 R157 W199 R200 Y217 Y296
Binding residue
(residue number reindexed from 1)		L10 G11 K12 Y13 I76 L77 P78 H82 E99 K100 R128 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1evj, PDBe:1evj, PDBj:1evj
PDBsum1evj
PubMed11099381
UniProtQ07982|GFO_ZYMMO Glucose--fructose oxidoreductase (Gene Name=gfo)

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