MolNFT v1 · #92312 · protein

Crystal structure of glmu from mycobacterium tuberculosis snapshot 3

4G3P · Bifunctional protein glmu: “Crystal structure of glmu from mycobacterium tuberculosis snapshot 3”. X-ray diffraction, 4 ligands (POP, UD1, MG), 3 pockets (best druggability 0.78). MolNFT v1 #92312 on GenesisL1: 3D structure, binding…

PDB: 4G3P
Type: protein
Length: 462 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: POP, UD1, MG, CO
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 23% 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	462	23% helix, 30% strand	P96382

Ligands and binding sites

POP · Pyrophosphate 2- · ligand · chains A
UD1 · Uridine-diphosphate-N-acetylglucosamine · 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	470	0.78	0.86	44	POP, CO, MG, UD1
2	170	0.44	0.74	15	empty
3	108	0.39	0.75	17	empty

Compared structures

4G3P · Crystal structure of GlmU from Mycobacterium tuberculosis Snapshot 3 · 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 4G3P · PDBe 4G3P · UniProt P96382

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