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Structure of the soluble domain of cytochrome C552 with its flexible linker segment from paracoccus denitrificans

Analyse Structure of the soluble domain of cytochrome C552 with its flexible linker… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3M97
Type
protein
Length
118 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C-552
UniProt
P54820
Ligands
HEC, ZN
Pockets
1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XCytochrome C-552protein11840% helix, 2% strandP54820

Ligands and binding sites

  • HEC · Heme C · ligand · chains X
  • ZN · Zinc ion · metal · 4 copies · chains X

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11870.770.9233HEC

Modifications

Observed in the structure: 2 cofactor (heme c attachment).

Compared structures

  • 3M97 · Structure of the soluble domain of cytochrome c552 with its flexible linker segment from… · the same entry in another collection · chain X against X, TM-score 1.00
  • P54820 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (P54820) · a predicted model of the same protein · chain X against A, TM-score 0.91

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