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Crystallographic and single crystal spectral analysis of the peroxidase ferryl intermediate

Analyse Crystallographic and single crystal spectral analysis of the peroxidase ferryl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3M26
Type
protein
Length
291 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C peroxidase, mitochondrial
EC
1.11.1.5
UniProt
P00431
Ligands
HEM, PO4
Pockets
2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACytochrome C peroxidase, mitochondrial (EC 1.11.1.5)protein29151% helix, 8% strandP00431

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • PO4 · Phosphate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13320.800.9043HEM
2960.410.7717empty

Compared structures

  • 3M26 · Crystallographic and Single Crystal Spectral Analysis of the Peroxidase Ferryl… · the same entry in another collection · chain A against A, TM-score 1.00
  • P00431 · AlphaFold monomer V2.0 prediction for cytochrome C peroxidase, mitochondrial (P00431) · a predicted model of the same protein · chain A against A, TM-score 1.00

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