Research workbench
Crystal strucuture of an inositol monophosphatase family protein (SAS2203) from staphylococcus aureus MSSA476
Analyse Crystal strucuture of an inositol monophosphatase family protein (SAS2203) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QMF
- Type
- protein
- Length
- 502 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
- SO4
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol monophosphatase family protein (EC 3.1.3.25) | protein | 254 | 35% helix, 26% strand | Q6G709 |
| B | Inositol monophosphatase family protein (EC 3.1.3.25) | protein | 248 | 30% helix, 25% strand | Q6G709 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.68 | 0.79 | 46 | SO4 |
| 2 | 318 | 0.58 | 0.77 | 37 | SO4 |
| 3 | 214 | 0.47 | 0.74 | 30 | empty |
| 4 | 175 | 0.44 | 0.74 | 25 | empty |
| 5 | 57 | 0.44 | 0.82 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1423 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 3QMF · Crystal strucuture of an inositol monophosphatase family protein (SAS2203) from… · 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 3QMF · PDBe 3QMF · UniProt Q6G709
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