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Crystal structure of mif L46F mutant

Analyse Crystal structure of mif L46F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EUI
Type: protein
Length: 342 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Macrophage migration inhibitory factor
EC: 5.3.2.1, 5.3.3.12
UniProt: P14174
Ligands: SO4
Pockets: 4 · best druggability 0.83

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Macrophage migration inhibitory factor (EC 5.3.2.1, 5.3.3.12)	protein	114	39% helix, 31% strand	P14174

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	479	0.83	0.90	50	empty
2	62	0.53	0.87	13	empty
3	53	0.49	0.86	13	empty
4	145	0.43	0.75	19	empty

Interfaces

3 interfaces between chains.

B–C · 1198 Å² buried · 19 hydrogen bonds · protein-protein
A–C · 1191 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1180 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

4EUI · Crystal Structure of MIF L46F mutant · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P14174
Elsewhere: RCSB PDB 4EUI · PDBe 4EUI · UniProt P14174

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