Research workbench
Crystal structure of staphylococcal inositol monophosphatase-1: 50MM licl inhibited complex
Analyse Crystal structure of staphylococcal inositol monophosphatase-1: 50MM licl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I40
- Type
- protein
- Length
- 524 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol monophosphatase family protein
- EC
- 3.1.3.25
- UniProt
- Q6G709
- Ligands
- MG, PO4
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Inositol monophosphatase family protein (EC 3.1.3.25) | protein | 262 | 36% helix, 26% strand | Q6G709 |
Ligands and binding sites
- MG · Magnesium ion · metal · 5 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 515 | 0.72 | 0.81 | 38 | MG, PO4, GOL |
| 2 | 464 | 0.70 | 0.81 | 36 | MG, PO4, GOL |
| 3 | 202 | 0.44 | 0.73 | 33 | PG4 |
| 4 | 143 | 0.37 | 0.72 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1553 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 4I40 · crystal structure of Staphylococcal inositol monophosphatase-1: 50mM LiCl inhibited… · the same entry in another collection · 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 Q6G709
- Elsewhere: RCSB PDB 4I40 · PDBe 4I40 · UniProt Q6G709
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