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Structure of four truncated and mutated forms of quenching protein

Analyse Structure of four truncated and mutated forms of quenching protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DJK
Type
protein
Length
515 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein suppressor of quenching 1, chloroplastic
EC
3.1.3.-
UniProt
Q8VZ10
Ligands
NA, CL
Pockets
7 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein suppressor of quenching 1, chloroplastic (EC 3.1.3.-)protein51516% helix, 37% strandQ8VZ10

Ligands and binding sites

  • NA · Sodium ion · metal · 5 copies · chains A
  • CL · Chloride ion · ion · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14110.710.8239empty
21670.630.8539CL
31760.520.7921empty
41520.430.7526empty
5540.350.7914empty

Compared structures

  • 7DJK · Structure of four truncated and mutated forms of quenching protein · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8VZ10 · AlphaFold monomer V2.0 prediction for protein suppressor of quenching 1, chloroplastic… · a predicted model of the same protein · chain A against A, TM-score 0.99

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