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Crystal structure of human myo-inositol monophosphatase 2 (IMPA2) with calcium and phosphate ions
Analyse Crystal structure of human myo-inositol monophosphatase 2 (IMPA2) with calcium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CZI
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol monophosphatase 2
- EC
- 3.1.3.25
- UniProt
- O14732
- Ligands
- CA, PO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol monophosphatase 2 (EC 3.1.3.25) | protein | 259 | 38% helix, 22% strand | O14732 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.57 | 0.86 | 19 | empty |
| 2 | 182 | 0.47 | 0.76 | 25 | CA, PO4 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2CZI · Crystal structure of human myo-inositol monophosphatase 2 (IMPA2) with calcium and… · 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 A against A, TM-score 0.96
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 2CZI · PDBe 2CZI · UniProt O14732
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