› 2v4m

X-ray diffraction
2.29Å resolution

The isomerase domain of human glutamine-fructose-6-phosphate transaminase 1 (GFPT1) in complex with fructose 6-phosphate

Released:
DOI: 10.2210/pdb2v4m/pdb
PDB entry 2v4m coloured by chain, front view.
PDB entry 2v4m coloured by chain, side view.
PDB entry 2v4m coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Moche M, Lehtio L, Andersson J, Arrowsmith CH, Berglund H, Collins R, Dahlgren LG, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Johansson A, Johansson I, Karlberg T, Kotenyova T, Nilsson ME, Nyman T, Persson C, Sagemark J, Svensson S, Schueler H, Thorsell AG, Tresaugues L, Uppenberg J, Van Den Berg S, Welin M, Wisniewska M, Weigelt J, Nordlund P, Wikstrom M

Function and Biology Details

Reaction catalysed: 
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170307 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 376 amino acids
Theoretical weight: 42.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06210 (Residues: 332-699; Coverage: 53%)
Gene names: GFAT, GFPT, GFPT1
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

2 bound ligands:
Ligand F6R 4 x F6R
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: R3
Unit cell:
a: 178.824Å b: 178.824Å c: 157.113Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.167 0.185
Expression system: Escherichia coli

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