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Crystal structure of a. fulgidus lon proteolytic domain

Analyse Crystal structure of a. fulgidus lon proteolytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Z0T
Type
protein
Length
1,174 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative protease la homolog type
EC
3.4.21.53
UniProt
O29883
Pockets
20 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, EPutative protease la homolog type (EC 3.4.21.53)protein19532% helix, 30% strandO29883
B, C, D, FPutative protease la homolog type (EC 3.4.21.53)protein19632% helix, 27% strandO29883

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14290.680.8052empty
23840.670.8046empty
31020.620.8826empty
43140.610.7844empty
5950.590.8723empty

Interfaces

6 interfaces between chains.

  • C–D · 963 Ų buried · 16 hydrogen bonds · protein-protein
  • A–F · 945 Ų buried · 17 hydrogen bonds · protein-protein
  • D–E · 930 Ų buried · 19 hydrogen bonds · protein-protein
  • A–B · 885 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 803 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 1Z0T · Crystal Structure of A. fulgidus Lon proteolytic domain · the same entry in another collection · chain F against F, TM-score 1.00
  • O29883 · AlphaFold monomer V2.0 prediction for archaeal lon protease (O29883) · a predicted model of the same protein · chain A against A, TM-score 0.92

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