Structure of PDB 1qfn Chain A Binding Site BS01

Receptor Information
>1qfn 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
>1qfn Chain B (length=25) Species: 562 (Escherichia coli) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
GAEDAQDDLVPSIQDDGSESGACKI
Receptor-Ligand Complex Structure
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PDB1qfn Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction.
ResolutionN/A
Binding residue
(original residue number in PDB)
C11 Y13 R16 R39 T44 K45 E46 T58 V59 P60 Y72 T73 A76 K80
Binding residue
(residue number reindexed from 1)
C11 Y13 R16 R39 T44 K45 E46 T58 V59 P60 Y72 T73 A76 K80
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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Biological Process

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Cellular Component
External links
PDB RCSB:1qfn, PDBe:1qfn, PDBj:1qfn
PDBsum1qfn
PubMed10493864
UniProtP68688|GLRX1_ECOLI Glutaredoxin 1 (Gene Name=grxA)

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