Research workbench
Mif with a allosteric inhibitor
Analyse Mif with a allosteric inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PEG
- Type
- protein
- Length
- 342 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14174
- Ligands
- 4FQ, SO4, PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E, F | — | protein | 114 | — | P14174 |
Ligands and binding sites
- 4FQ · 4-amino-5-hydroxy-6-[(E)-(3-{[3-(2-methylpropanoyl) pyrazolo[1,5-a]pyridin-2-yl]methyl}phenyl) diazenyl]naphthalene-1,3-disulfonic acid · ligand · chains E, F
- SO4 · Sulfate ion · ion · 3 copies · chains D, E, F
- PO4 · Phosphate ion · ion · 2 copies · chains E, F
- ACT · Acetate ion · additive · 4 copies · chains D, E, F
- GOL · Glycerol · additive · 2 copies · chains D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PEG · MIF with a allosteric inhibitor · the same entry in another collection · chain D against D, 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 6PEG · PDBe 6PEG · UniProt P14174
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