Structure of PDB 1geu Chain A Binding Site BS02

Receptor Information
>1geu Chain A (length=448) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKV
MWHAAQIREAIHMYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYENV
LGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVE
YGIDSDGFFALPALPERVAVVGAGYIGVELGGVINGLGAKTHLFEMFDAP
LPSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDGSLTLELEDGRSE
TVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVG
DNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTV
GLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKI
VGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR
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 chain1geu Chain A Residue 452 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1geu Anatomy of an engineered NAD-binding site.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		Y177 I178 E181 E197 M198 F199 A260 I261 G262 E309 L310 V342
Binding residue
(residue number reindexed from 1)		Y175 I176 E179 E195 M196 F197 A258 I259 G260 E307 L308 V340
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) L38 C42 C47 K50 Y177 E181 A437 H439 E444
Catalytic site (residue number reindexed from 1) L36 C40 C45 K48 Y175 E179 A435 H437 E442
Enzyme Commision number 1.8.1.7: glutathione-disulfide reductase.
Gene Ontology
Molecular Function
GO:0004362 glutathione-disulfide reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0050660 flavin adenine dinucleotide binding
GO:0050661 NADP binding
GO:0071949 FAD binding
Biological Process
GO:0006749 glutathione metabolic process
GO:0034599 cellular response to oxidative stress
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1geu, PDBe:1geu, PDBj:1geu
PDBsum1geu
PubMed7833810
UniProtP06715|GSHR_ECOLI Glutathione reductase (Gene Name=gor)

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