Structure of PDB 1m9h Chain A Binding Site BS01

Receptor Information
>1m9h Chain A (length=277) Species: 1720 (Corynebacterium sp.) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TVPSIVLNDGNSIPQLGYGVYKVPPADTQRAVEEALEVGYRHIDTAAIYG
NEEGVGAAIAASGIARDDLFITTKLWNDRHDGDEPAAAIAESLAKLALDQ
VDLYLVHWPTPAADNYVHAWEKMIELRAAGLTRSIGVSNHLVPHLERIVA
ATGVVPAVNQIELHPAYQQREITDWAAAHDVKIESWGPLGQGKYDLFGAE
PVTAAAAAHGKTPAQAVLRWHLQKGFVVFPGSVRREHLEENLDVFDFDLT
DTEIAAIDAMDPGDGSGRVSGHPDEVD
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 chain1m9h Chain A Residue 300 [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]
PDB1m9h Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G20 Y22 Y50 H108 Q161 W187 G188 P189 L190 Q192 A215 F230 P231 G232 H238 N242
Binding residue
(residue number reindexed from 1)		G19 Y21 Y49 H107 Q160 W186 G187 P188 L189 Q191 A214 F229 P230 G231 H237 N241
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) D45 Y50 K75 H108
Catalytic site (residue number reindexed from 1) D44 Y49 K74 H107
Enzyme Commision number 1.1.1.346: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming).
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Biological Process
GO:0019853 L-ascorbic acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1m9h, PDBe:1m9h, PDBj:1m9h
PDBsum1m9h
PubMed14718658
UniProtP06632|DKGA_CORSC 2,5-diketo-D-gluconic acid reductase A (Gene Name=dkgA)

[Back to BioLiP]