Research workbench

Free serine kinase (E30A mutant) in complex with phosphoserine and AMP

Analyse Free serine kinase (E30A mutant) in complex with phosphoserine and AMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5X0E
Type: protein
Length: 241 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Free serine kinase
UniProt: Q5JD03
Ligands: AMP, SEP, MG
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Free serine kinase	protein	241	34% helix, 27% strand	Q5JD03

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
SEP · Phosphoserine · ligand · chains A
MG · Magnesium ion · metal · 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	514	0.72	0.81	50	AMP, SEP, MG
2	83	0.35	0.75	17	empty

Compared structures

5X0E · Free serine kinase (E30A mutant) in complex with phosphoserine and AMP · the same entry in another collection · chain A against A, TM-score 1.00
Q5JD03 · AlphaFold monomer V2.0 prediction for L-serine kinase serk (Q5JD03) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 Q5JD03
Elsewhere: RCSB PDB 5X0E · PDBe 5X0E · UniProt Q5JD03

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