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Heterodimer constructed from pa cyt C551-ht cyt C552 and ht cyt C552- pa cyt C551 chimeric proteins

Analyse Heterodimer constructed from pa cyt C551-ht cyt C552 and ht cyt C552- pa cyt… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XEC
Type
protein
Length
162 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C-552,CYTOCHROME C-551; Cytochrome C-551,CYTOCHROME C-552
UniProt
P15452, P00099
Ligands
HEC
Pockets
2 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CCytochrome C-552,CYTOCHROME C-551protein8050% helix, 3% strandP15452, P00099
ACytochrome C-551,CYTOCHROME C-552protein8250% helix, 2% strandP15452, P00099

Ligands and binding sites

  • HEC · Heme C · ligand · 2 copies · chains C, 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12210.720.8734HEC
21980.700.8733HEC

Interfaces

1 interface between chains.

  • C–A · 1574 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

Compared structures

  • 5XEC · Heterodimer constructed from PA cyt c551-HT cyt c552 and HT cyt c552-PA cyt c551 chimeric… · the same entry in another collection · chain C against C, TM-score 1.00
  • P00099 · AlphaFold monomer V2.0 prediction for cytochrome C-551 (P00099) · a predicted model of the same protein · chain C against A, TM-score 0.75
  • P15452 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (P15452) · a predicted model of the same protein · chain C against A, TM-score 0.74

Analyse

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