Research workbench
Crystal structure of the ppm ser-thr phosphatase mspp from mycobacterium smegmatis in complex with sulfate
Analyse Crystal structure of the ppm ser-thr phosphatase mspp from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JFT
- Type
- protein
- Length
- 234 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ser-thr phosphatase mspp
- UniProt
- A0QTQ6
- Ligands
- MG, MN, SO4
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ser-thr phosphatase mspp | protein | 234 | 33% helix, 27% strand | A0QTQ6 |
Ligands and binding sites
- MG · Magnesium ion · metal · 5 copies · chains A
- MN · Manganese (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 282 | 0.66 | 0.82 | 38 | MG, SO4 |
Compared structures
- 2JFT · Crystal structure of the PPM Ser-Thr phosphatase MsPP from Mycobacterium smegmatis in… · 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 A0QTQ6
- Elsewhere: RCSB PDB 2JFT · PDBe 2JFT · UniProt A0QTQ6
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