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Crystal structure analysis of mglu in its tris form

Analyse Crystal structure analysis of mglu in its tris form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3IH9
Type
protein
Length
896 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Salt-tolerant glutaminase
EC
3.5.1.2
UniProt
Q4U1A6
Pockets
11 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSalt-tolerant glutaminase (EC 3.5.1.2)protein44846% helix, 16% strandQ4U1A6

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14050.630.7741empty
23980.630.7835empty
32330.470.7434empty
42200.460.7338empty
5650.410.8018empty

Interfaces

1 interface between chains.

  • A–B · 729 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 3IH9 · Crystal Structure Analysis of Mglu in its tris form · the same entry in another collection · chain B against B, TM-score 1.00

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