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AFGNA1 crystal structure complexed with acetyl-CoA and glucose-6P gives new insights into catalysis

Analyse AFGNA1 crystal structure complexed with acetyl-CoA and glucose-6P gives new… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VEZ
Type: protein
Length: 165 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glucosamine 6-phosphate acetyltransferase
EC: 2.3.1.4
UniProt: Q4WCU5
Ligands: ACO, G6P, PO4
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative glucosamine 6-phosphate acetyltransferase (EC 2.3.1.4)	protein	165	39% helix, 21% strand	Q4WCU5

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · chains A
G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · chains A
PO4 · Phosphate ion · ion

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	168	0.50	0.77	21	empty
2	153	0.49	0.78	18	empty
3	107	0.38	0.75	22	ACO

Compared structures

2VEZ · AfGNA1 crystal structure complexed with Acetyl-CoA and Glucose-6P gives new insights into… · 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 Q4WCU5
Elsewhere: RCSB PDB 2VEZ · PDBe 2VEZ · UniProt Q4WCU5

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