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The crystal structure of the bifunctional N-acetylglucosamine-1- phosphate URIDYLTRANSFERASE/GLUCOSAMINE-1-phosphate acetyltransferase from yersinia pestis CO92

Analyse The crystal structure of the bifunctional N-acetylglucosamine-1- phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FWW
Type: protein
Length: 445 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: A4TSJ5
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157)	protein	445	20% helix, 31% strand	A4TSJ5

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	591	0.66	0.76	56	empty
2	174	0.44	0.74	24	empty

Compared structures

3FWW · The crystal structure of the bifunctional N-acetylglucosamine-1-phosphate… · the same entry in another collection · chain A against A, TM-score 1.00
A4TSJ5 · AlphaFold monomer V2.0 prediction for bifunctional protein glmu (A4TSJ5) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 A4TSJ5
Elsewhere: RCSB PDB 3FWW · PDBe 3FWW · UniProt A4TSJ5

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