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Native structure of N-acetylglutamate synthase from Neisseria gonorrhoeae

Analyse Native structure of N-acetylglutamate synthase from Neisseria gonorrhoeae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2R8V
Type: protein
Length: 424 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.5
Source: Neisseria gonorrhoeae
Molecule: Putative acetylglutamate synthase
EC: 2.3.1.1
UniProt: Q5FAK7
Ligands: ACO
Pockets: 4 · best druggability 0.70

Structure

x-ray diffraction · resolution 2.5 · 1 distinct chain · 42% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative acetylglutamate synthase (EC 2.3.1.1)	protein	424	42% helix, 25% strand	Q5FAK7

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	315	0.70	0.83	46	ACO
2	224	0.66	0.84	40	empty
3	58	0.31	0.76	16	empty
4	67	0.30	0.73	12	empty

Compared structures

2R8V · Native structure of N-acetylglutamate synthase from neisseria gonorrhoeae · 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 Q5FAK7
Elsewhere: RCSB PDB 2R8V · PDBe 2R8V · UniProt Q5FAK7

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