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Human COA6: W59C mutant protein

Analyse Human COA6: W59C mutant protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PCF
Type
protein
Length
243 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C oxidase assembly factor 6 homolog
UniProt
Q5JTJ3
Pockets
4 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 84% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BCytochrome C oxidase assembly factor 6 homologprotein6585% helix, 0% strandQ5JTJ3
CCytochrome C oxidase assembly factor 6 homologprotein5684% helix, 0% strandQ5JTJ3
ACytochrome C oxidase assembly factor 6 homologprotein5883% helix, 0% strandQ5JTJ3
DCytochrome C oxidase assembly factor 6 homologprotein6483% helix, 0% strandQ5JTJ3

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18540.760.8062empty
24460.690.8028empty
32170.540.7726empty
4590.420.8122empty

Interfaces

5 interfaces between chains.

  • B–A · 671 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 482 Ų buried · 5 hydrogen bonds · protein-protein
  • A–D · 469 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 147 Ų buried · 1 hydrogen bond · protein-protein
  • C–D · 135 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 6PCF · Human Coa6: W59C mutant protein · the same entry in another collection · chain D against D, TM-score 1.00
  • Q5JTJ3 · AlphaFold monomer V2.0 prediction for cytochrome C oxidase assembly factor 6 homolog… · a predicted model of the same protein · chain D against A, TM-score 0.97

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