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Archaeal amino-terminal acetyltransferase (nat) bound to acetyl coenzyme a

Analyse Archaeal amino-terminal acetyltransferase (nat) bound to acetyl coenzyme a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LX9
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Archaeal amino-terminal acetyltransferase
EC: 2.3.1.-
UniProt: Q980R9
Ligands: ACO, ZN
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Archaeal amino-terminal acetyltransferase (EC 2.3.1.-)	protein	157	35% helix, 35% strand	Q980R9

Ligands and binding sites

ACO · Acetyl coenzyme *A · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	315	0.64	0.80	34	ACO

Compared structures

4LX9 · Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A · the same entry in another collection · chain A against A, TM-score 1.00
Q980R9 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase (Q980R9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q980R9
Elsewhere: RCSB PDB 4LX9 · PDBe 4LX9 · UniProt Q980R9

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