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Structure of acetylated Pig somatic Cytochrome c (Aly39) at 1.5A

Analyse Structure of acetylated Pig somatic Cytochrome c (Aly39) at 1.5A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8DVX
Type
protein
Length
416 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.5
Source
Sus scrofa
Molecule
Cytochrome c
UniProt
P62895
Ligands
FC6, HEC
Pockets
3 · best druggability 0.85

Structure

x-ray diffraction · resolution 1.5 · 1 distinct chain · 41% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DCytochrome cprotein10441% helix, 2% strandP62895

Ligands and binding sites

  • FC6 · Hexacyanoferrate(3-) · ligand · 7 copies · chains A, D, B, C
  • HEC · Heme C · ligand · 4 copies · chains A, D, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16900.850.8889HEC, FC6
26890.830.8690HEC, FC6
3560.250.7319empty

Interfaces

4 interfaces between chains.

  • B–C · 442 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 384 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 258 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 249 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 cofactor, 4 modified (heme c attachment, acetylation).

Compared structures

  • P62895 · AlphaFold monomer V2.0 prediction for cytochrome C (P62895) · a predicted model of the same protein · chain D against A, TM-score 0.99

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