4gro

X-ray diffraction
2Å resolution

Crystallographic and biological characterization of N- and C- terminus mutants of human MIF

Released:
Source organism: Homo sapiens
Entry authors: Fan C, Lolis E

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)
PDBe Complex ID:
PDB-CPX-146863 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage migration inhibitory factor Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 117 amino acids
Theoretical weight: 12.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14174 (Residues: 3-115; Coverage: 98%)
Gene names: GLIF, MIF, MMIF
Sequence domains: Macrophage migration inhibitory factor (MIF)
Structure domains: Macrophage Migration Inhibitory Factor

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: R3
Unit cell:
a: 156.96Å b: 156.96Å c: 96.121Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.188 0.23
Expression system: Escherichia coli BL21(DE3)