Research workbench
Crystal structure of Y36A mutant of human macrophage migration inhibitory factor
Analyse Crystal structure of Y36A mutant of human macrophage migration inhibitory factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BSI
- Type
- protein
- Length
- 912 residues
- Chains
- 8
- 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
- 13 · 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, D, E, F, G, J | 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 · 8 copies · chains A, B, C, D, E, F, G, J
- GOL · Glycerol · additive · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 470 | 0.83 | 0.90 | 47 | empty |
| 2 | 495 | 0.82 | 0.89 | 50 | empty |
| 3 | 249 | 0.60 | 0.80 | 35 | GOL |
| 4 | 268 | 0.60 | 0.79 | 35 | GOL |
| 5 | 137 | 0.60 | 0.84 | 24 | empty |
Interfaces
14 interfaces between chains.
- E–F · 1123 Ų buried · 16 hydrogen bonds · protein-protein
- D–F · 1121 Ų buried · 17 hydrogen bonds · protein-protein
- D–E · 1121 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 1111 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1110 Ų buried · 17 hydrogen bonds · protein-protein
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 5BSI · PDBe 5BSI · UniProt P14174
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.