Structure of PDB 1grx Chain A Binding Site BS01

Receptor Information
>1grx Chain A (length=85) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQTVIFGRSGCPYSVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQ
KAGKPVETVPQIFVDQQHIGGYTDFAAWVKENLDA
Ligand information
Ligand IDGSH
InChIInChI=1S/C10H17N3O6S/c11-5(10(18)19)1-2-7(14)13-6(4-20)9(17)12-3-8(15)16/h5-6,20H,1-4,11H2,(H,12,17)(H,13,14)(H,15,16)(H,18,19)/t5-,6-/m0/s1
InChIKeyRWSXRVCMGQZWBV-WDSKDSINSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(NCC(=O)O)C(NC(=O)CCC(C(=O)O)N)CS
OpenEye OEToolkits 1.7.6C(CC(=O)N[C@@H](CS)C(=O)NCC(=O)O)[C@@H](C(=O)O)N
CACTVS 3.370N[CH](CCC(=O)N[CH](CS)C(=O)NCC(O)=O)C(O)=O
CACTVS 3.370N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O)C(O)=O
OpenEye OEToolkits 1.7.6C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N
FormulaC10 H17 N3 O6 S
NameGLUTATHIONE
ChEMBLCHEMBL1543
DrugBankDB00143
ZINCZINC000003830891
PDB chain1grx Chain A Residue 86 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1grx NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
ResolutionN/A
Binding residue
(original residue number in PDB)		C11 Y13 S14 T58 V59
Binding residue
(residue number reindexed from 1)		C11 Y13 S14 T58 V59
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) R8 G10 C11 Y13 S14 K18 Y72
Catalytic site (residue number reindexed from 1) R8 G10 C11 Y13 S14 K18 Y72
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0009055 electron transfer activity
GO:0015035 protein-disulfide reductase activity
GO:0015036 disulfide oxidoreductase activity
GO:0015038 glutathione disulfide oxidoreductase activity
GO:0019153 protein-disulfide reductase (glutathione) activity
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process
GO:0010134 sulfate assimilation via adenylyl sulfate reduction
GO:0019345 cysteine biosynthetic process via S-sulfo-L-cysteine
GO:0034599 cellular response to oxidative stress
GO:0045454 cell redox homeostasis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1grx, PDBe:1grx, PDBj:1grx
PDBsum1grx
PubMed1304339
UniProtP68688|GLRX1_ECOLI Glutaredoxin 1 (Gene Name=grxA)

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