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Structure of the mitochondrial 2-cys peroxiredoxin from plasmodium falciparum

Analyse Structure of the mitochondrial 2-cys peroxiredoxin from plasmodium falciparum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C0D
Type: protein
Length: 343 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin peroxidase 2
EC: 1.11.1.7
UniProt: Q9BKL4
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin peroxidase 2 (EC 1.11.1.7)	protein	168	32% helix, 27% strand	Q9BKL4
B	Thioredoxin peroxidase 2 (EC 1.11.1.7)	protein	175	32% helix, 26% strand	Q9BKL4

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	453	0.72	0.82	66	empty
2	65	0.33	0.76	20	empty
3	50	0.30	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 1116 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2C0D · Structure of the mitochondrial 2-cys peroxiredoxin from Plasmodium falciparum · 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 Q9BKL4
Elsewhere: RCSB PDB 2C0D · PDBe 2C0D · UniProt Q9BKL4

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