Research workbench

Crystal structure of 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispe) from mycobacterium tuberculosis

Analyse Crystal structure of 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispe)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PYD
Type: protein
Length: 298 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
EC: 2.7.1.148
UniProt: P65178
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (EC 2.7.1.148)	protein	298	37% helix, 28% strand	P65178

Ligands and binding sites

GOL · Glycerol · 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	418	0.59	0.76	55	GOL

Compared structures

3PYD · crystal structure of 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (IspE) from… · 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 P65178
Elsewhere: RCSB PDB 3PYD · PDBe 3PYD · UniProt P65178

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.