MolNFT v1 · #92442 · protein

Crystal structure of glmu from mycobacterium tuberculosis snapshot 1

4G87 · Bifunctional protein glmu: “Crystal structure of glmu from mycobacterium tuberculosis snapshot 1”. X-ray diffraction, 4 ligands (UD1, POP, MG), 3 pockets (best druggability 0.78). MolNFT v1 #92442 on GenesisL1: 3D structure, binding…

PDB: 4G87
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: UD1, POP, MG, CO
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157)	protein	452	25% helix, 32% strand	P96382

Ligands and binding sites

UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · chains A
POP · Pyrophosphate 2- · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CO · Cobalt (II) ion · metal · 2 copies · 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	494	0.78	0.86	55	CO, MG, UD1, POP
2	129	0.41	0.75	17	empty
3	85	0.35	0.75	13	empty

Compared structures

4G87 · Crystal structure of GLMU from Mycobacterium tuberculosis snapshot 1 · 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 4G87 · PDBe 4G87 · UniProt P96382

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