Research workbench
Crystal structure of magnesium transporter mgte
Analyse Crystal structure of magnesium transporter mgte in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YVX
- Type
- protein
- Length
- 1,768 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MG2+ transporter mgte
- UniProt
- Q5SMG8
- Ligands
- MG
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | MG2+ transporter mgte | protein | 442 | 53% helix, 6% strand | Q5SMG8 |
Ligands and binding sites
- MG · Magnesium ion · metal · 18 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 969 | 0.86 | 0.87 | 123 | empty |
| 2 | 773 | 0.85 | 0.88 | 91 | MG |
| 3 | 509 | 0.81 | 0.87 | 76 | MG |
| 4 | 450 | 0.78 | 0.86 | 58 | MG |
| 5 | 360 | 0.75 | 0.86 | 47 | empty |
Interfaces
5 interfaces between chains.
- C–D · 5317 Ų buried · 62 hydrogen bonds · protein-protein
- A–B · 4978 Ų buried · 49 hydrogen bonds · protein-protein
- B–D · 568 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 113 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 101 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 Q5SMG8
- Elsewhere: RCSB PDB 2YVX · PDBe 2YVX · UniProt Q5SMG8
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