MolNFT v1 · #121445 · protein
Crystal structure of PRO1 deletion and M2A double mutant of macrophage migration inhibitory factor
5HVV: “Crystal structure of PRO1 deletion and M2A double mutant of macrophage migration inhibitory factor”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.86). MolNFT v1 #121445 on GenesisL1: 3D structure, binding sites…
- 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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