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The crystal structure of thioredoxin reductase from streptococcus pyogenes MGAS5005

Analyse The crystal structure of thioredoxin reductase from streptococcus pyogenes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UWY
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin reductase
EC: 1.8.1.9
UniProt: A0A0C6G0E1
Ligands: FAD, PO4
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin reductase (EC 1.8.1.9)	protein	306	28% helix, 29% strand	A0A0C6G0E1

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
PO4 · Phosphate ion · ion · 3 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	416	0.75	0.85	51	FAD
2	171	0.49	0.77	17	empty
3	65	0.38	0.79	15	empty
4	64	0.35	0.77	17	empty

Modifications

Observed in the structure: 8 modified, 1 disulfide (engineered, disulfide).

Compared structures

5UWY · The crystal structure of thioredoxin reductase from Streptococcus pyogenes MGAS5005 · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A0C6G0E1
Elsewhere: RCSB PDB 5UWY · PDBe 5UWY · UniProt A0A0C6G0E1

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