MolNFT v1 · #151572 · protein
Structure of the TRPML2 eld at pH 6.5
6HRR · Mucolipin-2: “Structure of the TRPML2 eld at pH 6.5”. X-ray diffraction, 2 ligands (K, CL), 4 pockets (best druggability 0.57). MolNFT v1 #151572 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6HRR
- Type
- protein
- Length
- 346 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mucolipin-2
- UniProt
- Q8IZK6
- Ligands
- K, CL
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mucolipin-2 | protein | 173 | 25% helix, 35% strand | Q8IZK6 |
| B | Mucolipin-2 | protein | 173 | 25% helix, 39% strand | Q8IZK6 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
- CL · Chloride ion · ion · 3 copies · chains A, B
- GOL · Glycerol · additive · 11 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.57 | 0.76 | 56 | MES, CL |
| 2 | 117 | 0.46 | 0.79 | 21 | empty |
| 3 | 69 | 0.41 | 0.80 | 13 | empty |
| 4 | 82 | 0.38 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 775 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q8IZK6
- Elsewhere: RCSB PDB 6HRR · PDBe 6HRR · UniProt Q8IZK6
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