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HTRA1 inactive protease domain S328A with carasil mutations D174R R274Q

Analyse HTRA1 inactive protease domain S328A with carasil mutations D174R R274Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Z0Y
Type
protein
Length
594 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serine protease HTRA1
EC
3.4.21.-
UniProt
Q92743
Ligands
SO4
Pockets
4 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 14% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerine protease HTRA1 (EC 3.4.21.-)protein20014% helix, 38% strandQ92743
BSerine protease HTRA1 (EC 3.4.21.-)protein19715% helix, 34% strandQ92743
CSerine protease HTRA1 (EC 3.4.21.-)protein19712% helix, 41% strandQ92743

Ligands and binding sites

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14650.670.7965empty
23050.570.7640empty
3680.380.7816empty
4510.270.7512SO4

Interfaces

3 interfaces between chains.

  • A–C · 500 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 323 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 271 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 6Z0Y · HtrA1 inactive protease domain S328A with CARASIL mutations D174R R274Q · the same entry in another collection · chain A against A, TM-score 1.00
  • Q92743 · AlphaFold monomer V2.0 prediction for serine protease HTRA1 (Q92743) · a predicted model of the same protein · chain B against A, TM-score 0.97

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