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Crystal structure of mif L46A mutant

Analyse Crystal structure of mif L46A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EVG
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: 3 · 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

3 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	501	0.83	0.89	56	empty
2	53	0.50	0.86	13	empty
3	172	0.43	0.74	18	empty

Interfaces

3 interfaces between chains.

A–C · 1093 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1088 Å² buried · 17 hydrogen bonds · protein-protein
B–C · 1087 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

4EVG · Crystal Structure of MIF L46A 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 4EVG · PDBe 4EVG · UniProt P14174

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