MolNFT v1 · #30177 · protein
Crystal structure of MTMR2 in complex with phosphatidylinositol 3,5- bisphosphate
1ZVR · Myotubularin-related protein 2: “Crystal structure of MTMR2 in complex with phosphatidylinositol 3,5- bisphosphate”. X-ray diffraction, 1 ligand (3PI), 4 pockets (best druggability 0.69). MolNFT v1 #30177 on GenesisL1: 3D structure…
- PDB
- 1ZVR
- Type
- protein
- Length
- 514 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
- 3PI
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myotubularin-related protein 2 (EC 3.1.3.-) | protein | 514 | 40% helix, 17% strand | Q13614 |
Ligands and binding sites
- 3PI · (1S)-2-(1-hydroxybutoxy)-1-{[(hydroxy{[(2r,3s,5r,6s)-2,4,6-trihydroxy-3,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl)oxy]methyl}ethyl butyrate · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.69 | 0.84 | 32 | EDO |
| 2 | 189 | 0.53 | 0.78 | 22 | empty |
| 3 | 244 | 0.51 | 0.75 | 34 | empty |
| 4 | 100 | 0.46 | 0.80 | 23 | 3PI |
Compared structures
- 1ZVR · Crystal Structure of MTMR2 in complex with phosphatidylinositol 3,5-bisphosphate · 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 1ZVR · PDBe 1ZVR · UniProt Q13614
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