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Crystal structure of the ppm ser-thr phosphatase mspp from mycobacterium smegmatis in complex with phosphate at 0.83 a resolution

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: 2JFR
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, CL, PO4
Pockets: 2 · best druggability 0.56

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 · 4 copies · chains A
MN · Manganese (II) ion · metal · chains A
CL · Chloride ion · ion · chains A
PO4 · Phosphate ion · ion · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.56	0.84	23	empty
2	107	0.37	0.75	18	MG, PO4

Compared structures

2JFR · 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 2JFR · PDBe 2JFR · UniProt A0QTQ6

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