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Cu-bound structure of an engineered metal-dependent protein trimer, TRICYT1

Analyse Cu-bound structure of an engineered metal-dependent protein trimer, TRICYT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6X8X
Type
protein
Length
106 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Soluble cytochrome B562
UniProt
P0ABE7
Ligands
HEC, CA, CU
Pockets
1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASoluble cytochrome B562protein10681% helix, 0% strandP0ABE7

Ligands and binding sites

  • HEC · Heme C · ligand · chains A
  • CA · Calcium ion · metal · 5 copies · chains A
  • CU · Copper (II) ion · metal · chains A

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
11430.620.8523HEC

Modifications

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

Compared structures

  • 6X8X · Cu-bound structure of an engineered metal-dependent protein trimer, TriCyt1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P0ABE7 · AlphaFold monomer V2.0 prediction for soluble cytochrome B562 (P0ABE7) · a predicted model of the same protein · chain A against A, TM-score 0.96

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