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Crystal structure of peroxiredoxin asp F3

Analyse Crystal structure of peroxiredoxin asp F3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5J9B
Type: protein
Length: 331 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peroxiredoxin asp F3
EC: 1.11.1.15
UniProt: O43099
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peroxiredoxin asp F3 (EC 1.11.1.15)	protein	163	26% helix, 25% strand	O43099
B	Peroxiredoxin asp F3 (EC 1.11.1.15)	protein	168	28% helix, 24% strand	O43099

Pockets

4 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	359	0.63	0.78	41	empty
2	300	0.57	0.77	40	empty
3	79	0.50	0.83	19	empty
4	72	0.34	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 752 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

5J9B · Crystal structure of peroxiredoxin Asp f3 · the same entry in another collection · chain A against A, TM-score 1.00
O43099 · AlphaFold monomer V2.0 prediction for peroxiredoxin asp F3 (O43099) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O43099
Elsewhere: RCSB PDB 5J9B · PDBe 5J9B · UniProt O43099

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