MolNFT v1 · #162289 · protein

Crystal structure of human gfat-1 G451E

6R4H · Glutamine--fructose-6-phosphate aminotransferase…: “Crystal structure of human gfat-1 G451E”. X-ray diffraction, 2 ligands (G6Q, GLU), 12 pockets (best druggability 0.87). MolNFT v1 #162289 on GenesisL1: 3D structure, binding sites…

PDB: 6R4H
Type: protein
Length: 1,320 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
EC: 2.6.1.16
UniProt: Q06210
Ligands: G6Q, GLU
Pockets: 12 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16)	protein	663	38% helix, 25% strand	Q06210
B	Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC 2.6.1.16)	protein	657	39% helix, 24% strand	Q06210

Ligands and binding sites

G6Q · Glucose-6-phosphate · ligand · 2 copies · chains A, B
GLU · Glutamic acid · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	634	0.87	0.92	56	empty
2	1024	0.80	0.82	89	G6Q, GLU
3	830	0.80	0.83	98	empty
4	125	0.79	0.98	26	G6Q
5	96	0.52	0.83	16	empty

Interfaces

1 interface between chains.

A–B · 2936 Å² buried · 57 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

6R4H · Crystal structure of human GFAT-1 G451E · the same entry in another collection · chain B against B, TM-score 1.00
Q06210 · AlphaFold monomer V2.0 prediction for glutamine--fructose-6-phosphate aminotransferase… · a predicted model of the same protein · chain B against A, TM-score 1.00

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 Q06210
Elsewhere: RCSB PDB 6R4H · PDBe 6R4H · UniProt Q06210

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