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Crystal structure of apo glutamine synthetase from dog ( canis familiaris)

Analyse Crystal structure of apo glutamine synthetase from dog ( canis familiaris) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2UU7
Type
protein
Length
5,550 residues
Chains
15
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamine synthetase
EC
6.3.1.2
UniProt
Q8HZM5
Ligands
MG, CL
Pockets
20 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, OGlutamine synthetase (EC 6.3.1.2)protein37029% helix, 25% strandQ8HZM5

Ligands and binding sites

  • MG · Magnesium ion · metal · 15 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O
  • CL · Chloride ion · ion · 15 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O

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
17620.760.81109empty
210190.760.78163empty
36870.760.8187MG
46740.750.8180MG
56260.750.8271MG

Interfaces

26 interfaces between chains.

  • L–M · 2158 Ų buried · 33 hydrogen bonds · protein-protein
  • F–G · 2157 Ų buried · 33 hydrogen bonds · protein-protein
  • G–H · 2151 Ų buried · 33 hydrogen bonds · protein-protein
  • N–O · 2150 Ų buried · 32 hydrogen bonds · protein-protein
  • I–J · 2148 Ų buried · 31 hydrogen bonds · protein-protein

Compared structures

  • 2UU7 · Crystal structure of apo glutamine synthetase from dog (Canis familiaris) · the same entry in another collection · chain O against O, TM-score 1.00

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