Research workbench
Characterization of N- and C- terminus mutants of human mif
Analyse Characterization of N- and C- terminus mutants of human mif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GRR
- Type
- protein
- Length
- 348 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
- AVR, CL, SO4
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 32% 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 | 116 | 38% helix, 32% strand | P14174 |
Ligands and binding sites
- AVR · (2R)-2-amino-1-[2-(1-methylethyl)pyrazolo[1,5-a]pyridin-3-yl]propan-1-one · ligand · chains B, C
- CL · Chloride ion · ion · 11 copies · chains A, B, C
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 688 | 0.82 | 0.86 | 71 | SO4, CL |
Interfaces
3 interfaces between chains.
- A–B · 1153 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1150 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 1144 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4GRR · characterization of N- and C- terminus mutants of human MIF · the same entry in another collection · chain A against A, TM-score 1.00
- P14174 · AlphaFold monomer V2.0 prediction for macrophage migration inhibitory factor (P14174) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 4GRR · PDBe 4GRR · UniProt P14174
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