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Crystal structure of mouse glutaminase C, L-glutamate-bound form

Analyse Crystal structure of mouse glutaminase C, L-glutamate-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3SS5
Type
protein
Length
1,571 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutaminase C
EC
3.5.1.2
UniProt
Q69ZX9
Ligands
GLU
Pockets
10 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 49% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutaminase C (EC 3.5.1.2)protein39450% helix, 12% strandQ69ZX9
BGlutaminase C (EC 3.5.1.2)protein39049% helix, 12% strandQ69ZX9
CGlutaminase C (EC 3.5.1.2)protein39649% helix, 12% strandQ69ZX9
DGlutaminase C (EC 3.5.1.2)protein39149% helix, 12% strandQ69ZX9

Ligands and binding sites

  • GLU · Glutamic acid · ligand · 4 copies · chains A, B, C, D

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110270.760.79120GLU
29930.750.78108GLU
33760.710.8342empty
43750.690.8242empty
5990.370.7517empty

Interfaces

4 interfaces between chains.

  • B–C · 1704 Ų buried · 23 hydrogen bonds · protein-protein
  • A–D · 1687 Ų buried · 24 hydrogen bonds · protein-protein
  • C–D · 494 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 470 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 3SS5 · Crystal structure of mouse Glutaminase C, L-glutamate-bound form · the same entry in another collection · chain A against A, TM-score 1.00

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