GL1X · GenesisL1 explorer

Research workbench

Crystal structure of argininosuccinate lyase from mycobacterium tuberculosis

Analyse Crystal structure of argininosuccinate lyase from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IG5
Type
protein
Length
1,820 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Argininosuccinate lyase
EC
4.3.2.1
UniProt
P9WPY7
Pockets
18 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DArgininosuccinate lyase (EC 4.3.2.1)protein45569% helix, 5% strandP9WPY7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17230.790.8466empty
27300.790.8377empty
37580.780.8265empty
47740.770.8166empty
53140.610.7843empty

Interfaces

6 interfaces between chains.

  • B–D · 4060 Ų buried · 66 hydrogen bonds · protein-protein
  • A–C · 3961 Ų buried · 70 hydrogen bonds · protein-protein
  • C–D · 1774 Ų buried · 33 hydrogen bonds · protein-protein
  • A–B · 1762 Ų buried · 31 hydrogen bonds · protein-protein
  • A–D · 1744 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 6IG5 · Crystal structure of argininosuccinate lyase from Mycobacterium tuberculosis · the same entry in another collection · chain D against D, TM-score 1.00
  • P9WPY7 · AlphaFold monomer V2.0 prediction for argininosuccinate lyase (P9WPY7) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.