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L. monocytogenes GS(12) - apo

Analyse L. monocytogenes GS(12) - apo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7TFE
Type
protein
Length
5,316 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamine synthetase
EC
6.3.1.2
UniProt
A0A5D5GA79
Ligands
MG
Pockets
20 · best druggability 0.79

Structure

electron microscopy · 1 distinct chain · 39% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, G, H, I, B, C, J, D, E, F, K, LGlutamine synthetase (EC 6.3.1.2)protein44339% helix, 21% strandA0A5D5GA79

Ligands and binding sites

  • MG · Magnesium ion · metal · 24 copies · chains A, G, H, I, B, C, J, D, E, F, K, L

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
17070.790.8372empty
27030.780.8363empty
37060.780.8266empty
46620.780.8369empty
56800.770.8365empty

Interfaces

24 interfaces between chains.

  • A–F · 2165 Ų buried · 20 hydrogen bonds · protein-protein
  • G–L · 2165 Ų buried · 18 hydrogen bonds · protein-protein
  • I–J · 2153 Ų buried · 21 hydrogen bonds · protein-protein
  • C–D · 2147 Ų buried · 21 hydrogen bonds · protein-protein
  • H–K · 2141 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 7TFE · L. monocytogenes GS(12) - apo · the same entry in another collection · chain A against A, TM-score 1.00

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