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The crystal structure of thymidylate kinase from Pseudomonas aeruginosa PAO1 in complex with deoxythymidine.

Analyse The crystal structure of thymidylate kinase from Pseudomonas aeruginosa PAO1 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ESH
Type: protein
Length: 207 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.95
Source: Pseudomonas aeruginosa
Molecule: Thymidylate kinase
EC: 2.7.4.9
UniProt: Q9HZN8
Ligands: THM
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · resolution 1.95 · 1 distinct chain · 54% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate kinase (EC 2.7.4.9)	protein	207	54% helix, 13% strand	Q9HZN8

Ligands and binding sites

THM · Thymidine · ligand · chains A

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

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	289	0.72	0.86	37	THM

Compared structures

4ESH · The crystal structure of thymidylate kinase from pseudomonas aeruginosa PAO1 in complex… · the same entry in another collection · chain A against A, TM-score 1.00
Q9HZN8 · AlphaFold monomer V2.0 prediction for thymidylate kinase (Q9HZN8) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9HZN8
Elsewhere: RCSB PDB 4ESH · PDBe 4ESH · UniProt Q9HZN8

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