Structure of PDB 3uko Chain A Binding Site BS03

Receptor Information
>3uko Chain A (length=378) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATQGQVITCKAAVAYEPNKPLVIEDVQVAPPQAGEVRIKILYTALCHTDA
YTWSGKDPEGLFPCILGHEAAGIVESVGEGVTEVQAGDHVIPCYQAECRE
CKFCKSGKTNLCGKVRSATGVGIMMNDRKSRFSVNGKPIYHFMGTSTFSQ
YTVVHDVSVAKIDPTAPLDKVCLLGCGVPTGLGAVWNTAKVEPGSNVAIF
GLGTVGLAVAEGAKTAGASRIIGIDIDSKKYETAKKFGVNEFVNPKDHDK
PIQEVIVDLTDGGVDYSFECIGNVSVMRAALECCHKGWGTSVIVGVAASG
QEISTRPFQLVTGRVWKGTAFGGFKSRTQVPWLVEKYMNKEIKVDEYITH
NLTLGEINKAFDLLHEGTCLRCVLDTSK
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 chain3uko Chain A Residue 402 [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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PDB3uko Crystal structure and kinetic behavior of alcohol dehydrogenase III /S-nitrosoglutathione reductase from arabidopsis thaliana
Resolution1.4 Å
Binding residue
(original residue number in PDB)		H48 T181 G204 V206 D226 I227 K231 C271 I272 V295 G296 V297 A321
Binding residue
(residue number reindexed from 1)		H47 T180 G203 V205 D225 I226 K230 C270 I271 V294 G295 V296 A320
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) C47 H48 T49 Y52 H69 E70 C99 C102 C105 C113 R117 C177 T181 R372
Catalytic site (residue number reindexed from 1) C46 H47 T48 Y51 H68 E69 C98 C101 C104 C112 R116 C176 T180 R371
Enzyme Commision number 1.1.1.-
1.1.1.1: alcohol dehydrogenase.
1.1.1.284: S-(hydroxymethyl)glutathione dehydrogenase.
Gene Ontology
Molecular Function
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051903 S-(hydroxymethyl)glutathione dehydrogenase [NAD(P)+] activity
GO:0080007 S-nitrosoglutathione reductase (NADH) activity
GO:0106321 S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity
GO:0106322 S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity
Biological Process
GO:0044281 small molecule metabolic process
GO:0046294 formaldehyde catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3uko, PDBe:3uko, PDBj:3uko
PDBsum3uko
PubMed
UniProtQ96533|ADHX_ARATH Alcohol dehydrogenase class-3 (Gene Name=ADH2)

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