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Mutant M58C of nostoc sp cytochrome C6

Analyse Mutant M58C of nostoc sp cytochrome C6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4H0J
Type
protein
Length
516 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C6
UniProt
P0A3X7
Ligands
HEC
Pockets
7 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FCytochrome C6protein8660% helix, 5% strandP0A3X7

Ligands and binding sites

  • HEC · Heme C · ligand · 6 copies · chains A, B, C, D, E, F

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

Pockets

7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19820.890.91116HEC
22600.730.8735HEC
32660.730.8638HEC
42310.730.8728HEC
52330.710.8630HEC

Interfaces

12 interfaces between chains.

  • B–F · 439 Ų buried · 2 hydrogen bonds · protein-protein
  • C–D · 428 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 428 Ų buried · 2 hydrogen bonds · protein-protein
  • C–E · 426 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 328 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 cofactor (heme c attachment).

Compared structures

  • 4H0J · Mutant M58C of Nostoc sp Cytochrome c6 · the same entry in another collection · chain F against F, TM-score 1.00
  • P0A3X7 · AlphaFold monomer V2.0 prediction for cytochrome C6 (P0A3X7) · a predicted model of the same protein · chain F against A, TM-score 0.99

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