9cxw

X-ray diffraction
1.8Å resolution

Crystal structure of Human FN3K bound with ADP and DMF (II)

Released:
Source organism: Homo sapiens
Entry authors: Garg A, On KF, Joshua-Tor L

Function and Biology Details

Reactions catalysed:
ATP + [protein]-N(6)-D-fructosyl-L-lysine = ADP + [protein]-N(6)-(3-O-phospho-D-fructosyl)-L-lysine
ATP + [protein]-N(6)-D-ribulosyl-L-lysine = ADP + [protein]-N(6)-(3-O-phospho-D-ribulosyl)-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-282978 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructosamine-3-kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 291 amino acids
Theoretical weight: 33.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H479 (Residues: 1-116, 139-309; Coverage: 93%)
Gene name: FN3K
Sequence domains: Fructosamine kinase

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 52.854Å b: 111.765Å c: 132.661Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.22
Expression system: Escherichia coli