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Allosteric inhibition of kidney isoform of glutaminase

Analyse Allosteric inhibition of kidney isoform of glutaminase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JYP
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutaminase kidney isoform, mitochondrial
EC: 3.5.1.2
UniProt: O94925
Ligands: ZBS
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutaminase kidney isoform, mitochondrial (EC 3.5.1.2)	protein	308	49% helix, 14% strand	O94925

Ligands and binding sites

ZBS · 2-phenyl-~{N}-[5-[(1~{S},3~{S})-3-[5-(2-phenylethanoylamino)-1,3,4-thiadiazol-2-yl]cyclohexyl]-1,3,4-thiadiazol-2-yl]ethanamide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	278	0.55	0.76	33	empty

Compared structures

5JYP · Allosteric inhibition of Kidney Isoform of Glutaminase · the same entry in another collection · chain A against A, TM-score 1.00
O94925 · AlphaFold monomer V2.0 prediction for glutaminase kidney isoform, mitochondrial (O94925) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O94925
Elsewhere: RCSB PDB 5JYP · PDBe 5JYP · UniProt O94925

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