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2.3 ångström crystal structure of a glucose-1-phosphate thymidylyltransferase from bacillus anthracis in complex with thymidine-5-diphospho-alpha-D-glucose and pyrophosphate

Analyse 2.3 ångström crystal structure of a glucose-1-phosphate thymidylyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ECM
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-1-phosphate thymidylyltransferase
EC: 2.7.7.24
UniProt: Q81TP2
Ligands: DAU, POP
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24)	protein	245	30% helix, 29% strand	Q81TP2

Ligands and binding sites

DAU · 2'deoxy-thymidine-5'-diphospho-alpha-D-glucose · ligand · chains A
POP · Pyrophosphate 2- · 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	372	0.76	0.86	43	DAU, POP

Compared structures

4ECM · 2.3 Angstrom Crystal Structure of a Glucose-1-phosphate Thymidylyltransferase 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 Q81TP2
Elsewhere: RCSB PDB 4ECM · PDBe 4ECM · UniProt Q81TP2

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