Research workbench
Crystal structure of inositol polyphosphate 1-phosphatase at 2.3 ångströms resolution
Analyse Crystal structure of inositol polyphosphate 1-phosphatase at 2.3 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1INP
- Type
- protein
- Length
- 400 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol polyphosphate 1-phosphatase
- EC
- 3.1.3.57
- UniProt
- P21327
- Ligands
- MG
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol polyphosphate 1-phosphatase (EC 3.1.3.57) | protein | 400 | 29% helix, 20% strand | P21327 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.74 | 0.81 | 53 | MG |
| 2 | 267 | 0.59 | 0.79 | 37 | empty |
| 3 | 143 | 0.55 | 0.81 | 30 | empty |
| 4 | 74 | 0.44 | 0.81 | 20 | empty |
| 5 | 99 | 0.38 | 0.76 | 17 | empty |
Compared structures
- 1INP · Crystal structure of inositol polyphosphate 1-phosphatase at 2.3 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P21327 · AlphaFold monomer V2.0 prediction for inositol polyphosphate 1-phosphatase (P21327) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P21327
- Elsewhere: RCSB PDB 1INP · PDBe 1INP · UniProt P21327
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