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The structure of oxidized rat cytochrome C at 1.13 ångströms resolution

Analyse The structure of oxidized rat cytochrome C at 1.13 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5C0Z
Type
protein
Length
416 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C, somatic
UniProt
P62898
Ligands
HEC, FC6
Pockets
5 · best druggability 0.83

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DCytochrome C, somaticprotein10441% helix, 2% strandP62898

Ligands and binding sites

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16720.830.8786HEC, FC6
26520.820.8790HEC, FC6
3650.280.7318empty
4560.270.7418empty
5570.260.7314empty

Interfaces

4 interfaces between chains.

  • A–D · 445 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 418 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 223 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 193 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 cofactor (heme c attachment).

Compared structures

  • 5C0Z · The structure of oxidized rat cytochrome c at 1.13 angstroms resolution · the same entry in another collection · chain D against D, TM-score 1.00
  • P62898 · AlphaFold monomer V2.0 prediction for cytochrome C, somatic (P62898) · a predicted model of the same protein · chain B against A, TM-score 0.99

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