GL1X · GenesisL1 explorer

Research workbench

The structure of the macrophage migration inhibitory factor from trichinella spiralis.

Analyse The structure of the macrophage migration inhibitory factor from trichinella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HFO
Type
protein
Length
678 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Migration inhibitory factor
UniProt
Q9Y063
Pockets
8 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FMigration inhibitory factorprotein11339% helix, 31% strandQ9Y063

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15450.800.8659empty
25170.790.8652empty
3690.630.9115empty
4520.520.8816empty
5560.500.8616empty

Interfaces

6 interfaces between chains.

  • A–C · 1148 Ų buried · 21 hydrogen bonds · protein-protein
  • E–F · 1138 Ų buried · 20 hydrogen bonds · protein-protein
  • D–F · 1133 Ų buried · 22 hydrogen bonds · protein-protein
  • B–C · 1119 Ų buried · 19 hydrogen bonds · protein-protein
  • A–B · 1103 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 1HFO · The Structure of the Macrophage Migration Inhibitory Factor from Trichinella Spiralis. · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.