Research workbench
Crystal structure of PRO1 deletion and M2A double mutant of macrophage migration inhibitory factor
Analyse Crystal structure of PRO1 deletion and M2A double mutant of macrophage… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HVV
- Type
- protein
- Length
- 339 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
- SO4
- Pockets
- 1 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 30% 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 | 113 | 39% helix, 30% strand | P14174 |
Ligands and binding sites
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 | 941 | 0.86 | 0.87 | 101 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1079 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1060 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1047 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 5HVV · Crystal structure of Pro1 deletion and M2A double mutant of Macrophage Migration… · the same entry in another collection · chain A against A, 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 5HVV · PDBe 5HVV · UniProt P14174
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