Structure of PDB 1cqg Chain A

Receptor sequence

>1cqgA (length=105) Species: 9606 (Homo sapiens) [Search protein sequence]

MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPAKMIKPFFHSLSEKYS
NVIFLEVDVDDAQDVASEAEVKATPTFQFFKKGQKVGEFSGANKEKLEAT
INELV

3D structure

PDB

1cqg The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.

Chain

Resolution

N/A

3D
structure

Catalytic site residues are labeled in the structure
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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	?

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	peptide	A	W31 C32 V59 D60 V71 K72 A73 T74 G91 A92	W31 C32 V59 D60 V71 K72 A73 T74 G91 A92

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

External links

PDB	RCSB:1cqg, PDBe:1cqg, PDBj:1cqg
PDBsum	1cqg
PubMed	8736558
UniProt	P10599\|THIO_HUMAN Thioredoxin (Gene Name=TXN)