MolNFT v1 · #30082 · protein
Crystal structure of MTMR2 in complex with phosphatidylinositol 3- phosphate
1ZSQ · Myotubularin-related protein 2: “Crystal structure of MTMR2 in complex with phosphatidylinositol 3- phosphate”. X-ray diffraction, 1 ligand (PIB), 6 pockets (best druggability 0.69). MolNFT v1 #30082 on GenesisL1: 3D structure…
- PDB
- 1ZSQ
- Type
- protein
- Length
- 513 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myotubularin-related protein 2
- EC
- 3.1.3.-
- UniProt
- Q13614
- Ligands
- PIB
- Pockets
- 6 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myotubularin-related protein 2 (EC 3.1.3.-) | protein | 513 | 39% helix, 17% strand | Q13614 |
Ligands and binding sites
- PIB · 2-(butanoyloxy)-1-{[(hydroxy{[2,3,4,6-tetrahydroxy-5-(phosphonooxy)cyclohexyl]oxy}phosphoryl) oxy]methyl}ethyl butanoate · ligand · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 282 | 0.69 | 0.84 | 31 | EDO |
| 2 | 54 | 0.59 | 0.91 | 21 | empty |
| 3 | 188 | 0.53 | 0.78 | 22 | empty |
| 4 | 176 | 0.44 | 0.74 | 23 | empty |
| 5 | 92 | 0.39 | 0.77 | 19 | PIB |
Compared structures
- 1ZSQ · Crystal Structure of MTMR2 in complex with phosphatidylinositol 3-phosphate · the same entry in another collection · chain A against A, TM-score 1.00
- Q13614 · AlphaFold monomer V2.0 prediction for myotubularin-related protein 2 (Q13614) · a predicted model of the same protein · 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 Q13614
- Elsewhere: RCSB PDB 1ZSQ · PDBe 1ZSQ · UniProt Q13614
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