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Crystal structure of human myo-inositol monophosphatase 2 (IMPA2) (orthorhombic form)
Analyse Crystal structure of human myo-inositol monophosphatase 2 (IMPA2) (orthorhombic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DDK
- Type
- protein
- Length
- 507 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol monophosphatase 2
- EC
- 3.1.3.25
- UniProt
- O14732
- Pockets
- 6 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol monophosphatase 2 (EC 3.1.3.25) | protein | 258 | 38% helix, 24% strand | O14732 |
| B | Inositol monophosphatase 2 (EC 3.1.3.25) | protein | 249 | 36% helix, 25% strand | O14732 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.65 | 0.80 | 45 | empty |
| 2 | 268 | 0.62 | 0.81 | 33 | empty |
| 3 | 251 | 0.62 | 0.81 | 31 | empty |
| 4 | 118 | 0.57 | 0.84 | 23 | empty |
| 5 | 169 | 0.46 | 0.76 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1511 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2DDK · Crystal structure of human myo-inositol monophosphatase 2 (IMPA2) (orthorhombic form) · the same entry in another collection · chain A against A, TM-score 1.00
- O14732 · AlphaFold monomer V2.0 prediction for inositol monophosphatase 2 (O14732) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 O14732
- Elsewhere: RCSB PDB 2DDK · PDBe 2DDK · UniProt O14732
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