Research workbench

Structure of the phosphatase domain of the cell fate determinant spoiie from bacillus subtilis in a crystal form without domain swapping

Analyse Structure of the phosphatase domain of the cell fate determinant spoiie from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MQH
Type: protein
Length: 228 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serine phosphatase
UniProt: A0A0D1KMY9
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine phosphatase	protein	228	28% helix, 31% strand	A0A0D1KMY9

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	155	0.54	0.80	26	empty

Compared structures

5MQH · Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus… · 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 A0A0D1KMY9
Elsewhere: RCSB PDB 5MQH · PDBe 5MQH · UniProt A0A0D1KMY9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.