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Crystal structure of escherichia COLI thiol peroxidase in the oxidized state

Analyse Crystal structure of escherichia COLI thiol peroxidase in the oxidized state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QXH
Type: protein
Length: 328 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thiol peroxidase
EC: 1.11.1.-
UniProt: P0A862
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thiol peroxidase (EC 1.11.1.-)	protein	164	18% helix, 31% strand	P0A862

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	158	0.51	0.78	23	empty
2	169	0.50	0.77	25	empty
3	142	0.49	0.79	28	empty

Interfaces

1 interface between chains.

A–B · 719 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1QXH · Crystal Structure of Escherichia coli Thiol Peroxidase in the Oxidized State · the same entry in another collection · chain A against A, TM-score 1.00
P0A862 · AlphaFold monomer V2.0 prediction for thiol peroxidase (P0A862) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P0A862
Elsewhere: RCSB PDB 1QXH · PDBe 1QXH · UniProt P0A862

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