Research workbench
Crystal structure of INPP5B in complex with phosphatidylinositol 3,4- bisphosphate
Analyse Crystal structure of INPP5B in complex with phosphatidylinositol 3,4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CML
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type II inositol 1,4,5-trisphosphate 5- phosphatase, isoform 2
- EC
- 3.1.3.36
- UniProt
- P32019
- Ligands
- 52N, MG, CL, SO4
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type II inositol 1,4,5-trisphosphate 5- phosphatase, isoform 2 (EC 3.1.3.36) | protein | 310 | 22% helix, 36% strand | P32019 |
Ligands and binding sites
- 52N · 1,2-dioctanoyl phosphatidyl epi-inositol (3,4)-bisphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.30 | 0.75 | 18 | MG |
Compared structures
- 4CML · Crystal Structure of INPP5B in complex with Phosphatidylinositol 3,4- bisphosphate · the same entry in another collection · chain A against A, TM-score 1.00
- P32019 · AlphaFold monomer V2.0 prediction for type II inositol 1,4,5-trisphosphate 5-phosphatase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P32019
- Elsewhere: RCSB PDB 4CML · PDBe 4CML · UniProt P32019
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