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A double mutant of dsbg engineered for denitrosylation

Analyse A double mutant of dsbg engineered for denitrosylation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5G1L
Type
protein
Length
456 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Thiol disulfide interchange protein dsbg
UniProt
P77202
Ligands
SO4
Pockets
3 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BThiol disulfide interchange protein dsbgprotein22838% helix, 24% strandP77202

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12200.830.9633empty
21460.450.7626empty
31090.410.7720empty

Interfaces

1 interface between chains.

  • A–B · 1624 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 5G1L · A double mutant of DsbG engineered for denitrosylation · the same entry in another collection · chain A against A, TM-score 1.00
  • P77202 · AlphaFold monomer V2.0 prediction for THIOL:DISULFIDE interchange protein dsbg (P77202) · a predicted model of the same protein · chain B against A, TM-score 0.98

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