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Time-resolved structural snapshot of proteolysis by glpg inside the membrane

Analyse Time-resolved structural snapshot of proteolysis by glpg inside the membrane in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PJQ
Type
protein
Length
178 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rhomboid protease glpg; Peptide aldehyde inhibitor
EC
3.4.21.105
UniProt
A0A0J2E248
Pockets
1 · best druggability 0.32

Structure

x-ray diffraction · 2 distinct chains · 76% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARhomboid protease glpg (EC 3.4.21.105)protein17379% helix, 2% strandA0A0J2E248
BPeptide aldehyde inhibitorprotein50% helix, 40% strand—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1660.320.7418empty

Interfaces

1 interface between chains.

  • A–B · 547 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6PJQ · Time-resolved structural snapshot of proteolysis by GlpG inside the membrane · the same entry in another collection · chain A against A, TM-score 1.00

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