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Crystal structure of full-length human peroxiredoxin 4 in three different redox states

Analyse Crystal structure of full-length human peroxiredoxin 4 in three different redox… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TKS
Type
protein
Length
985 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peroxiredoxin-4
EC
1.11.1.15
UniProt
Q13162
Ligands
PER

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EPeroxiredoxin-4 (EC 1.11.1.15)protein19730% helix, 25% strandQ13162

Ligands and binding sites

  • PER · Peroxide ion · ion · 3 copies · chains A, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

5 interfaces between chains.

  • C–D · 67 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 67 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 66 Ų buried · 0 hydrogen bonds · protein-protein
  • D–E · 65 Ų buried · 0 hydrogen bonds · protein-protein
  • A–E · 63 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (oxidation).

Compared structures

  • 3TKS · Crystal structure of full-length human peroxiredoxin 4 in three different redox states · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13162 · AlphaFold monomer V2.0 prediction for peroxiredoxin-4 (Q13162) · a predicted model of the same protein · chain A against A, TM-score 0.99

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