MolNFT v1 · #50129 · protein

Crystal structure of N-acetylglutamate synthase (selenomet substituted) from neisseria gonorrhoeae

2R98 · Putative acetylglutamate synthase: “Crystal structure of N-acetylglutamate synthase (selenomet substituted) from neisseria gonorrhoeae”. X-ray diffraction, 1 ligand (ACO), 5 pockets (best druggability 0.64). MolNFT v1 #50129 on…

PDB: 2R98
Type: protein
Length: 424 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative acetylglutamate synthase
EC: 2.3.1.1
UniProt: Q5FAK7
Ligands: ACO
Pockets: 5 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative acetylglutamate synthase (EC 2.3.1.1)	protein	424	42% helix, 26% 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

5 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	218	0.64	0.83	37	ACO
2	213	0.64	0.83	45	empty
3	99	0.42	0.77	17	empty
4	74	0.34	0.76	23	empty
5	52	0.28	0.74	12	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2R98 · Crystal Structure of N-acetylglutamate synthase (selenoMet substituted) from Neisseria… · 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 2R98 · PDBe 2R98 · UniProt Q5FAK7

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