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Crystal structure of hamster mif

Analyse Crystal structure of hamster mif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ICE
Type
protein
Length
344 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Macrophage migration inhibitory factor
UniProt
A0A140EDM8
Pockets
3 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMacrophage migration inhibitory factorprotein11638% helix, 30% strandA0A140EDM8
B, CMacrophage migration inhibitory factorprotein11439% helix, 31% strandA0A140EDM8

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16120.820.8767empty
2520.540.8812empty
3580.510.8613empty

Interfaces

3 interfaces between chains.

  • B–C · 1137 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 1122 Ų buried · 19 hydrogen bonds · protein-protein
  • A–C · 1106 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 6ICE · Crystal structure of Hamster MIF · the same entry in another collection · chain A against A, TM-score 1.00

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