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X-ray diffraction
1.9Å resolution

HUMAN GLYCOSYLATION-INHIBITING FACTOR

Released:

Function and Biology Details

Reactions catalysed:
Keto-phenylpyruvate = enol-phenylpyruvate
L-dopachrome = 5,6-dihydroxyindole-2-carboxylate

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage migration inhibitory factor Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 115 amino acids
Theoretical weight: 12.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14174 (Residues: 1-115; Coverage: 100%)
Gene names: GLIF, MIF, MMIF
Sequence domains: Macrophage migration inhibitory factor (MIF)
Structure domains: Macrophage Migration Inhibitory Factor

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 96.6Å b: 96.6Å c: 105.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Escherichia coli