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Oxidised thiol peroxidase (tpx) from yersinia pseudotuberculosis

Analyse Oxidised thiol peroxidase (tpx) from yersinia pseudotuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XPE
Type: protein
Length: 330 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thiol peroxidase
EC: 1.11.1.-
UniProt: Q66A71
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thiol peroxidase (EC 1.11.1.-)	protein	164	18% helix, 29% strand	Q66A71
B	Thiol peroxidase (EC 1.11.1.-)	protein	166	20% helix, 31% strand	Q66A71

Pockets

3 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	165	0.50	0.78	20	empty
2	172	0.47	0.75	22	empty
3	165	0.46	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 657 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2XPE · Oxidised Thiol peroxidase (Tpx) from Yersinia pseudotuberculosis · 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 Q66A71
Elsewhere: RCSB PDB 2XPE · PDBe 2XPE · UniProt Q66A71

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