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A fully oxidized human thioredoxin

Analyse A fully oxidized human thioredoxin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DQY
Type: protein
Length: 105 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin
UniProt: P10599
Ligands: BEZ, CL

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin	protein	105	38% helix, 26% strand	P10599

Ligands and binding sites

BEZ · Benzoic acid · ligand · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

5DQY · A fully oxidized human thioredoxin · the same entry in another collection · chain A against A, TM-score 1.00
P10599 · AlphaFold monomer V2.0 prediction for thioredoxin (P10599) · a predicted model of the same protein · chain A against A, TM-score 0.95

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P10599
Elsewhere: RCSB PDB 5DQY · PDBe 5DQY · UniProt P10599

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