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Crystal structure of probable phosphoserine phosphatase from vibrio cholerae, unliganded form

Analyse Crystal structure of probable phosphoserine phosphatase from vibrio cholerae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N28
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoserine phosphatase
UniProt: Q9KPM2
Ligands: SO4
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoserine phosphatase	protein	323	44% helix, 21% strand	Q9KPM2

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 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	141	0.71	0.90	25	empty
2	96	0.46	0.80	17	empty
3	56	0.36	0.79	12	empty

Compared structures

3N28 · Crystal structure of probable phosphoserine phosphatase from vibrio cholerae, unliganded… · the same entry in another collection · chain A against A, TM-score 1.00
Q9KPM2 · AlphaFold monomer V2.0 prediction for phosphoserine phosphatase (Q9KPM2) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q9KPM2
Elsewhere: RCSB PDB 3N28 · PDBe 3N28 · UniProt Q9KPM2

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