Research workbench
Macrophage migration inhibitory factor from ancylostoma ceylanicum
Analyse Macrophage migration inhibitory factor from ancylostoma ceylanicum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OS5
- Type
- protein
- Length
- 472 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acemif
- UniProt
- A4GRE3
- Ligands
- SO4
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Acemif | protein | 118 | 41% helix, 26% strand | A4GRE3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.76 | 0.97 | 26 | empty |
| 2 | 203 | 0.52 | 0.77 | 18 | empty |
| 3 | 103 | 0.50 | 0.81 | 20 | empty |
| 4 | 107 | 0.50 | 0.81 | 21 | empty |
| 5 | 119 | 0.44 | 0.77 | 21 | empty |
Interfaces
5 interfaces between chains.
- B–D · 1282 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1219 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 1206 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 810 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 181 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2OS5 · Macrophage migration inhibitory factor from Ancylostoma ceylanicum · 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 A4GRE3
- Elsewhere: RCSB PDB 2OS5 · PDBe 2OS5 · UniProt A4GRE3
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