Research workbench
Crystallographic and biological characterization of N- and C- terminus mutants of human mif
Analyse Crystallographic and biological characterization of N- and C- terminus mutants… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GRP
- Type
- protein
- Length
- 352 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, CL
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrophage migration inhibitory factor (EC 5.3.2.1, 5.3.3.12) | protein | 118 | 37% helix, 31% strand | P14174 |
| B, C | Macrophage migration inhibitory factor (EC 5.3.2.1, 5.3.3.12) | protein | 117 | 38% helix, 32% strand | P14174 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 496 | 0.83 | 0.90 | 53 | SO4 |
| 2 | 110 | 0.35 | 0.72 | 18 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1124 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1120 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 1116 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4GRP · Crystallographic and biological characterization of N- and C- terminus mutants of human… · the same entry in another collection · chain B against B, 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 4GRP · PDBe 4GRP · UniProt P14174
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.