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S.PNEUMONIAE glmu complexed with udp-N-acetylglucosamine and MG2+

Analyse S.PNEUMONIAE glmu complexed with udp-N-acetylglucosamine and MG2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G97
Type: protein
Length: 446 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acetylglucosamine-1-phosphate uridyltransferase
EC: 2.7.7.23
UniProt: Q97R46
Ligands: UD1, MG, NA
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acetylglucosamine-1-phosphate uridyltransferase (EC 2.7.7.23)	protein	446	23% helix, 31% strand	Q97R46

Ligands and binding sites

UD1 · Uridine-diphosphate-N-acetylglucosamine · ligand · chains A
MG · Magnesium ion · metal · chains A
NA · Sodium ion · metal · 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	693	0.78	0.82	57	MG, UD1
2	65	0.32	0.75	15	empty

Compared structures

1G97 · S.PNEUMONIAE glmu complexed with udp-N-acetylglucosamine and MG2+ · the same entry in another collection · chain A against A, TM-score 1.00
Q97R46 · AlphaFold monomer V2.0 prediction for bifunctional protein glmu (Q97R46) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q97R46
Elsewhere: RCSB PDB 1G97 · PDBe 1G97 · UniProt Q97R46

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