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The structure of oxidized rat cytochrome C (T28A) at 1.362 ångströms resolution.

Analyse The structure of oxidized rat cytochrome C (T28A) at 1.362 ångströms resolution. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5C9M
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
4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DCytochrome C, somaticprotein10442% 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16870.830.8688HEC, FC6
26560.820.8691HEC, FC6
3690.290.7316empty
4510.260.7415empty

Interfaces

4 interfaces between chains.

  • B–C · 431 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 389 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 223 Ų buried · 5 hydrogen bonds · protein-protein
  • C–D · 185 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 5C9M · The structure of oxidized rat cytochrome c (T28A) at 1.362 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 D against A, TM-score 0.99

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