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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
1Z0G
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
19 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, EPutative protease la homolog type (EC 3.4.21.53)protein19536% helix, 29% strandO29883
B, C, D, FPutative protease la homolog type (EC 3.4.21.53)protein19633% helix, 28% strandO29883

Pockets

19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14260.680.8046empty
24020.680.8055empty
33390.620.7953empty
41060.590.8626empty
5870.590.8720empty

Interfaces

6 interfaces between chains.

  • D–E · 953 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 941 Ų buried · 17 hydrogen bonds · protein-protein
  • A–F · 920 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 918 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 870 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 1Z0G · 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 B against A, TM-score 0.92

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