Research workbench
Human macrophage migration inhibitory factor (mif)
Analyse Human macrophage migration inhibitory factor (mif) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GD0
- Type
- protein
- Length
- 350 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Macrophage migration inhibitory factor
- UniProt
- P14174
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Macrophage migration inhibitory factor | protein | 118 | 37% helix, 30% strand | P14174 |
| B | Macrophage migration inhibitory factor | protein | 114 | 39% helix, 31% strand | P14174 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, C, B
- CIT · Citric acid · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 499 | 0.84 | 0.90 | 52 | CIT |
| 2 | 62 | 0.55 | 0.87 | 13 | empty |
| 3 | 68 | 0.51 | 0.85 | 13 | empty |
| 4 | 57 | 0.49 | 0.85 | 13 | empty |
| 5 | 165 | 0.44 | 0.74 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1244 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1223 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1177 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 1GD0 · Human macrophage migration inhibitory factor (mif) · the same entry in another collection · chain C against C, 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 1GD0 · PDBe 1GD0 · UniProt P14174
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