Structure of PDB 1tde Chain A

Receptor sequence

>1tdeA (length=316) Species: 562 (Escherichia coli)

GTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVE
NWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLNGDN
GEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAV
IGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNII
LHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGLFVAIGHSPNTA
IFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAG
TGCMAALDAERYLDGL

3D structure

• PDB: 1tde Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis.
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C135 C138 D139
• Catalytic site (residue number reindexed from 1): C135 C138 D139
• Enzyme Commision number: 1.8.1.9: thioredoxin-disulfide reductase.

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	FAD	A	G12 S13 G14 P15 A16 T35 G36 E38 G41 Q42 L43 T46 V49 N51 H83 I84 A111 T112 G113 C138 G285 D286 R293 Q294 A295 S298	G12 S13 G14 P15 A16 T35 G36 E38 G41 Q42 L43 T46 V49 N51 H83 I84 A111 T112 G113 C138 G285 D286 R293 Q294 A295 S298

Gene Ontology

Molecular Function

• GO:0004791 thioredoxin-disulfide reductase (NADPH) activity
• GO:0005515 protein binding
• GO:0016491 oxidoreductase activity
• GO:0050660 flavin adenine dinucleotide binding

Biological Process

• GO:0019430 removal of superoxide radicals
• GO:0045454 cell redox homeostasis

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:1902515 thioredoxin-disulfide reductase complex

External links

• PDB: RCSB:1tde, PDBe:1tde, PDBj:1tde
• PDBsum: 1tde
• PubMed: 8114095
• UniProt: P0A9P4|TRXB_ECOLI Thioredoxin reductase (Gene Name=trxB)