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Crystal structure of macrophage migration inhibitory factor in complex with btzo-14
Analyse Crystal structure of macrophage migration inhibitory factor in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B4O
- 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
- 6DQ, SO4
- Pockets
- 4 · best druggability 0.80
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
- 6DQ · 2-pyridin-3-yl-1,3-benzothiazin-4-one · ligand · 4 copies · chains A, B, C
- SO4 · Sulfate ion · ion · 9 copies · chains A, B, C
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 545 | 0.80 | 0.87 | 61 | SO4 |
| 2 | 64 | 0.50 | 0.84 | 12 | 6DQ |
| 3 | 56 | 0.49 | 0.85 | 12 | 6DQ |
| 4 | 70 | 0.46 | 0.82 | 16 | 6DQ |
Interfaces
3 interfaces between chains.
- A–C · 1152 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1152 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 1133 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 5B4O · Crystal structure of Macrophage Migration Inhibitory Factor in complex with BTZO-14 · 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 5B4O · PDBe 5B4O · UniProt P14174
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