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Crystal structure of a. fulgidus RIO2 serine protein kinase bound to ATP

Analyse Crystal structure of a. fulgidus RIO2 serine protein kinase bound to ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TQP
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Conserved hypothetical protein
UniProt: O30245
Ligands: ATP
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Conserved hypothetical protein	protein	269	45% helix, 22% strand	O30245

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 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	283	0.59	0.78	32	ATP
2	58	0.35	0.77	13	empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

1TQP · Crystal Structure of A. fulgidus Rio2 Serine Protein Kinase Bound to ATP · the same entry in another collection · chain A against A, TM-score 1.00
O30245 · AlphaFold monomer V2.0 prediction for rio-type SERINE/THREONINE- protein kinase RIO2… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O30245
Elsewhere: RCSB PDB 1TQP · PDBe 1TQP · UniProt O30245

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