Structure of PDB 1cqh Chain A Binding Site BS01
Receptor Information
>1cqh Chain A (length=105) Species:
9606
(Homo sapiens) [
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MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPAKMIKPFFHSLSEKYS
NVIFLEVDVDDAQDVASEAEVKATPTFQFFKKGQKVGEFSGANKEKLEAT
INELV
Ligand information
>1cqh Chain B (length=13) Species:
9606
(Homo sapiens) [
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PATLKICSWNVDG
Receptor-Ligand Complex Structure
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PDB
1cqh
The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.
Resolution
N/A
Binding residue
(original residue number in PDB)
W31 C32 V59 V71 K72 A73 T74 G91
Binding residue
(residue number reindexed from 1)
W31 C32 V59 V71 K72 A73 T74 G91
Enzymatic activity
Catalytic site (original residue number in PDB)
C32 G33 P34 A35
Catalytic site (residue number reindexed from 1)
C32 G33 P34 A35
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0003723
RNA binding
GO:0004791
thioredoxin-disulfide reductase (NADPH) activity
GO:0005515
protein binding
GO:0015035
protein-disulfide reductase activity
GO:0042803
protein homodimerization activity
GO:0047134
protein-disulfide reductase (NAD(P)H) activity
Biological Process
GO:0000122
negative regulation of transcription by RNA polymerase II
GO:0009314
response to radiation
GO:0033138
positive regulation of peptidyl-serine phosphorylation
GO:0043388
positive regulation of DNA binding
GO:0045454
cell redox homeostasis
GO:0046826
negative regulation of protein export from nucleus
GO:0051897
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
GO:0061692
cellular detoxification of hydrogen peroxide
GO:0071731
response to nitric oxide
GO:2000170
positive regulation of peptidyl-cysteine S-nitrosylation
Cellular Component
GO:0005576
extracellular region
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0070062
extracellular exosome
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Cellular Component
External links
PDB
RCSB:1cqh
,
PDBe:1cqh
,
PDBj:1cqh
PDBsum
1cqh
PubMed
8736558
UniProt
P10599
|THIO_HUMAN Thioredoxin (Gene Name=TXN)
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