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Structural comparison between aspergillus fumigatus and human GNA1

Analyse Structural comparison between aspergillus fumigatus and human GNA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VXK
Type: protein
Length: 165 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucosamine 6-phosphate acetyltransferase
EC: 2.3.1.4
UniProt: Q4WCU5
Ligands: 16G, COA, PO4
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucosamine 6-phosphate acetyltransferase (EC 2.3.1.4)	protein	165	37% helix, 21% strand	Q4WCU5

Ligands and binding sites

16G · 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-glucopyranose · ligand · chains A
COA · Coenzyme A · ligand · chains A
PO4 · Phosphate ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.49	0.77	22	empty
2	129	0.49	0.79	17	empty
3	129	0.41	0.74	26	16G, COA

Compared structures

2VXK · Structural comparison between Aspergillus fumigatus and human GNA1 · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q4WCU5
Elsewhere: RCSB PDB 2VXK · PDBe 2VXK · UniProt Q4WCU5

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