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Crystal structure of glucosamine-1-phosphate N-acetyltransferase from stenotrophomonas maltophilia K279A

Analyse Crystal structure of glucosamine-1-phosphate N-acetyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7K47
Type: protein
Length: 455 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: B2FHY5
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional protein glmu (EC 2.7.7.23, 2.3.1.157)	protein	455	21% helix, 35% strand	B2FHY5

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	472	0.61	0.75	53	empty
2	126	0.40	0.74	23	empty
3	59	0.32	0.76	22	empty

Compared structures

7K47 · Crystal Structure of Glucosamine-1-phosphate N-acetyltransferase from Stenotrophomonas… · the same entry in another collection · chain A against A, TM-score 1.00
B2FHY5 · AlphaFold monomer V2.0 prediction for bifunctional protein glmu (B2FHY5) · 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 B2FHY5
Elsewhere: RCSB PDB 7K47 · PDBe 7K47 · UniProt B2FHY5

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