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Thymidine kinase from B. cereus with ttp bound as phosphate donor.

Analyse Thymidine kinase from B. cereus with ttp bound as phosphate donor. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JA1
Type: protein
Length: 193 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidine kinase
EC: 2.7.1.21
UniProt: Q0H9H6
Ligands: TTP, ZN
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidine kinase (EC 2.7.1.21)	protein	193	21% helix, 28% strand	Q0H9H6

Ligands and binding sites

TTP · Thymidine-5'-triphosphate · ligand · chains A
ZN · Zinc ion · metal · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 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	288	0.68	0.83	40	TTP, MPD

Compared structures

2JA1 · Thymidine kinase from B. cereus with TTP bound as phosphate donor. · 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 Q0H9H6
Elsewhere: RCSB PDB 2JA1 · PDBe 2JA1 · UniProt Q0H9H6

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