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Htra proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues

Analyse Htra proteases are activated by a conserved mechanism that can be triggered by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MH4
Type
protein
Length
684 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protease do
EC
3.4.21.-
UniProt
P0C0V0
Pockets
10 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtease do (EC 3.4.21.-)protein30114% helix, 36% strandP0C0V0
BProtease do (EC 3.4.21.-)protein38315% helix, 36% strandP0C0V0

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11360.730.9226empty
23360.670.8147empty
3510.670.9626empty
41090.570.8527empty
52110.550.7829empty

Interfaces

1 interface between chains.

  • A–B · 530 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 3MH4 · HtrA proteases are activated by a conserved mechanism that can be triggered by distinct… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0C0V0 · AlphaFold monomer V2.0 prediction for periplasmic serine endoprotease degp (P0C0V0) · a predicted model of the same protein · chain A against A, TM-score 0.77

Analyse

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