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Lon protease from thermus thermophilus

Analyse Lon protease from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7P6U
Type
protein
Length
4,639 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lon protease; (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)
EC
3.4.21.53
UniProt
Q9LCX1
Ligands
ANP
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 3 distinct chains · 41% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, D, E, FLon protease (EC 3.4.21.53)protein77242% helix, 16% strandQ9LCX1
CLon protease (EC 3.4.21.53)protein77241% helix, 15% strandQ9LCX1
S(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)protein70% helix, 14% strand—

Ligands and binding sites

  • ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 5 copies · chains A, B, C, D, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19860.840.85122empty
29830.840.85102empty
39290.840.85109ANP
411520.810.83105empty
56890.810.8655ANP

Interfaces

20 interfaces between chains.

  • B–C · 4126 Ų buried · 56 hydrogen bonds · protein-protein
  • C–D · 3804 Ų buried · 64 hydrogen bonds · protein-protein
  • A–B · 3785 Ų buried · 59 hydrogen bonds · protein-protein
  • D–E · 3482 Ų buried · 39 hydrogen bonds · protein-protein
  • A–F · 3027 Ų buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 7P6U · Lon protease from Thermus Thermophilus · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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