› 2oow

X-ray diffraction
1.75Å resolution

Function and Biology Details

Reactions catalysed: 
Keto-phenylpyruvate = enol-phenylpyruvate
L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146863 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage migration inhibitory factor Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 114 amino acids
Theoretical weight: 12.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14174 (Residues: 2-115; Coverage: 99%)
Gene names: GLIF, MIF, MMIF
Sequence domains: Macrophage migration inhibitory factor (MIF)
Structure domains: Macrophage Migration Inhibitory Factor

Ligands and Environments

4 bound ligands:
Ligand SO4 5 x SO4
Ligand OX4 2 x OX4
Ligand GOL 6 x GOL
Ligand IPA 3 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU, null
Spacegroup: P212121
Unit cell:
a: 67.61Å b: 67.794Å c: 87.248Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Orthologs of macrophage migration inhibitory factor from parasitic nematodes.
Vermeire et al. (2008)
5 more

2 mentions without citation

Alternative chemical modifications reverse the binding orientation of a pharmacophore scaffold in the active site of macrophage migration inhibitory factor.
Crichlow et al. (2007)
1 more