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Crystal structure of human glutaminase in complex with L-glutamine

Analyse Crystal structure of human glutaminase in complex with L-glutamine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VP0
Type: protein
Length: 310 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: GLN, SO4
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutaminase kidney isoform, mitochondrial (EC 3.5.1.2)	protein	310	48% helix, 13% strand	O94925

Ligands and binding sites

GLN · Glutamine · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	340	0.61	0.78	41	GLN
2	61	0.36	0.78	19	empty

Compared structures

3VP0 · Crystal structure of human glutaminase in complex with L-glutamine · 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 3VP0 · PDBe 3VP0 · UniProt O94925

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