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The 5-coordinate proximal no complex of cytochrome C prime from shewanella frigidimarina

Analyse The 5-coordinate proximal no complex of cytochrome C prime from shewanella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CX9
Type
protein
Length
256 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C, class II
UniProt
Q07Z15
Ligands
HEC, NO, SO4
Pockets
2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCytochrome C, class IIprotein12871% helix, 2% strandQ07Z15

Ligands and binding sites

  • HEC · Heme C · ligand · 2 copies · chains A, B
  • NO · Nitric oxide · ion · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • GOL · Glycerol · additive · 5 copies · chains A, B

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
12210.650.8324HEC, NO
22220.630.8225NO, HEC

Interfaces

1 interface between chains.

  • A–B · 747 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 4CX9 · The 5-coordinate proximal NO complex of cytochrome c prime from Shewanella frigidimarina · the same entry in another collection · chain A against A, TM-score 1.00

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