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Crystal Structure of GTP-bound Irgb6_T95D mutant

Analyse Crystal Structure of GTP-bound Irgb6_T95D mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8H4M
Type: protein
Length: 406 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.68
Source: Mus musculus
Molecule: T-cell-specific guanine nucleotide triphosphate-binding protein 2
EC: 3.6.5.-
UniProt: Q3T9E4
Ligands: GTP
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · resolution 1.68 · 1 distinct chain · 55% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T-cell-specific guanine nucleotide triphosphate-binding protein 2 (EC 3.6.5.-)	protein	406	55% helix, 9% strand	Q3T9E4

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	112	0.62	0.87	28	empty
2	202	0.52	0.77	29	empty
3	53	0.48	0.85	13	empty
4	99	0.40	0.76	19	empty
5	59	0.30	0.75	11	empty

Compared structures

Q3T9E4 · AlphaFold monomer V2.0 prediction for T-cell-specific guanine nucleotide… · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q3T9E4
Elsewhere: RCSB PDB 8H4M · PDBe 8H4M · UniProt Q3T9E4

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