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Tetrameric allochromatium vinosum cytochrome C'

Analyse Tetrameric allochromatium vinosum cytochrome C' in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GYR
Type
protein
Length
1,048 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C'
UniProt
P00154
Ligands
HEC
Pockets
16 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, E, F, I, J, M, NCytochrome C'protein13171% helix, 5% strandP00154

Ligands and binding sites

  • HEC · Heme C · ligand · 8 copies · chains A, N, B, E, J, F, I, M

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

Pockets

16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17000.790.8394empty
22610.760.8934HEC
37930.760.8077HEC
48200.760.8084HEC
52620.750.8835HEC

Interfaces

13 interfaces between chains.

  • E–J · 2686 Ų buried · 27 hydrogen bonds · protein-protein
  • A–N · 2683 Ų buried · 24 hydrogen bonds · protein-protein
  • I–J · 845 Ų buried · 7 hydrogen bonds · protein-protein
  • M–N · 833 Ų buried · 8 hydrogen bonds · protein-protein
  • E–F · 813 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 cofactor (heme c attachment).

Compared structures

  • 5GYR · Tetrameric Allochromatium vinosum cytochrome c' · the same entry in another collection · chain J against J, TM-score 1.00
  • P00154 · AlphaFold monomer V2.0 prediction for cytochrome C' (P00154) · a predicted model of the same protein · chain F against A, TM-score 0.99

Analyse

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