MolNFT v2 · #63939 · protein

Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.

3FOQ · Bifunctional protein glmU: “Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis…”. X-ray diffraction at 3.41, 1 ligand (SO4), 2 pockets (best druggability 0.64). MolNFT v2…

PDB: 3FOQ
Type: protein
Length: 439 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.41
Source: Mycobacterium tuberculosis
Molecule: Bifunctional protein glmU
EC: 2.7.7.23, 2.3.1.157
UniProt: P96382
Ligands: SO4
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · resolution 3.41 · 1 distinct chain · 21% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional protein glmU (EC 2.7.7.23, 2.3.1.157)	protein	439	21% helix, 30% strand	P96382

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · 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	496	0.64	0.76	45	empty
2	127	0.41	0.75	21	empty

Compared structures

3FOQ · Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (glmu) 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 P96382
Elsewhere: RCSB PDB 3FOQ · PDBe 3FOQ · UniProt P96382

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