MolNFT v1 · #8140 · protein

N-acetyl-L-glutamate kinase from escherichia COLI complexed with its substrate N-acetylglutamate and its substrate analog amppnp

1GS5 · Acetylglutamate kinase: “N-acetyl-L-glutamate kinase from escherichia COLI complexed with its substrate N-acetylglutamate and its…”. X-ray diffraction, 3 ligands (NLG, ANP, MG), 4 pockets (best druggability 0.65). MolNFT v1 #8140 on…

PDB: 1GS5
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylglutamate kinase
EC: 2.7.2.8
UniProt: P11445
Ligands: NLG, ANP, MG
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetylglutamate kinase (EC 2.7.2.8)	protein	258	45% helix, 23% strand	P11445

Ligands and binding sites

NLG · N-acetyl-L-glutamate · ligand · chains A
ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	304	0.65	0.81	38	NLG, ANP, MG
2	74	0.36	0.77	16	empty
3	60	0.33	0.77	13	empty
4	73	0.32	0.74	21	empty

Compared structures

1GS5 · N-acetyl-L-glutamate kinase from Escherichia coli complexed with its substrate… · 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 P11445
Elsewhere: RCSB PDB 1GS5 · PDBe 1GS5 · UniProt P11445

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