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Crystal structure of glmu from mycobacterium tuberculosis in complex with glucosamine-1-phosphate

Analyse Crystal structure of glmu from mycobacterium tuberculosis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HCQ
Type: protein
Length: 452 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional protein glmu
EC: 2.7.7.23, 2.3.1.157
UniProt: P96382
Ligands: GN1, MG, CO
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157)	protein	452	24% helix, 33% strand	P96382

Ligands and binding sites

GN1 · 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose · ligand · 2 copies · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CO · Cobalt (II) ion · metal · chains A

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

Pockets

3 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	543	0.76	0.83	45	GN1, MG
2	121	0.40	0.75	16	empty
3	80	0.36	0.76	18	empty

Compared structures

4HCQ · Crystal structure of GLMU from mycobacterium tuberculosis in complex with… · 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 4HCQ · PDBe 4HCQ · UniProt P96382

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