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Glutathione peroxidase-type tryparedoxin peroxidase, oxidized form

Analyse Glutathione peroxidase-type tryparedoxin peroxidase, oxidized form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DWV
Type: protein
Length: 326 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione peroxidase-like protein
EC: 1.11.1.9
UniProt: Q869A5
Pockets: 5 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione peroxidase-like protein (EC 1.11.1.9)	protein	163	28% helix, 20% strand	Q869A5

Pockets

5 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	184	0.54	0.79	36	empty
2	131	0.49	0.79	25	empty
3	85	0.38	0.77	16	empty
4	113	0.35	0.73	22	empty
5	66	0.31	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 641 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3DWV · Glutathione peroxidase-type tryparedoxin peroxidase, oxidized form · the same entry in another collection · chain A against A, TM-score 1.00

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 Q869A5
Elsewhere: RCSB PDB 3DWV · PDBe 3DWV · UniProt Q869A5

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