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Copper resistance protein copg- form 2

Analyse Copper resistance protein copg- form 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WJE
Type
protein
Length
754 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DUF411 domain-containing protein
UniProt
A0A5C0YHL7
Ligands
ZN, CU
Pockets
7 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, D, E, FDUF411 domain-containing proteinprotein12625% helix, 35% strandA0A5C0YHL7
CDUF411 domain-containing proteinprotein12425% helix, 35% strandA0A5C0YHL7

Ligands and binding sites

  • ZN · Zinc ion · metal · 35 copies · chains A, B, C, D, E, F
  • CU · Copper (II) ion · metal · 20 copies · chains A, B, C, D, E, F
  • ACT · Acetate ion · additive · 3 copies · chains A, B, C, D

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12560.530.7628ZN
22890.530.7536ZN
3710.440.8122empty
4600.400.8118ACT
5500.390.8116empty

Interfaces

5 interfaces between chains.

  • B–C · 598 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 585 Ų buried · 15 hydrogen bonds · protein-protein
  • E–F · 546 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 524 Ų buried · 14 hydrogen bonds · protein-protein
  • B–E · 37 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 modified (disulfide, oxidation).

Compared structures

  • 6WJE · Copper resistance protein copG- Form 2 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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