Research workbench
Structure of a membrane protein
Analyse Structure of a membrane protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U9N
- Type
- protein
- Length
- 355 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Magnesium transporter mgte
- UniProt
- Q5SMG8
- Ligands
- OLA, MN
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Magnesium transporter mgte | protein | 177 | 87% helix, 0% strand | Q5SMG8 |
| B | Magnesium transporter mgte | protein | 178 | 88% helix, 0% strand | Q5SMG8 |
Ligands and binding sites
- OLA · Oleic acid · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.80 | 0.96 | 40 | MN |
| 2 | 317 | 0.61 | 0.78 | 43 | empty |
Interfaces
1 interface between chains.
- A–B · 2937 Ų buried · 37 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 4U9N · PDBe 4U9N · UniProt Q5SMG8
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